Infobox protein family Symbol GATase Name Glutamine amidotransferase class I image PDB 1o1y EBI.jpg width caption crystal structure of putative glutamine amido transferase tm1158 from thermotoga maritima at 1.70 a resolution Pfam PF00117 Pfam clan CL0014 InterPro IPR000991 SMART PROSITE PDOC00406 MEROPS C44 SCOP 1ea0 TCDB OPM family OPM protein CAZy CDD In molecular biology, glutamine amidotransferases GATase are enzymes which catalyse the removal of the ammonia group from a glutamic acid glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon nitrogen group on the Enzyme substrate substrate . This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase component II, p aminobenzoate, and glutamine dependent carbamoyl transferase CPSase . Glutamine amidotransferase GATase protein domain domains can occur either as single polypeptides, as in glutamine amidotransferases, or as protein domains domains in a much larger multifunctional synthase protein, such as CPSase. On the basis of sequence biology sequence similarities two classes of GATase domains have been identified class I also known as trpG type and class II also known as purF type ref name pmid3298209 cite journal author Weng ML, Zalkin H title Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain journal J. Bacteriol. volume 169 issue 7 pages 3023 8 year 1987 month July pmid 3298209 pmc 212343 doi url ref ref name pmid6086650 cite journal author Nyunoya H, Lusty CJ title Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain journal J. Biol. Chem. volume 259 issue 15 pages 9790 8 year 1984 month August pmid 6086650 doi url ref . Class I GATase domains are defined by a conserved sequence conserved catalytic triad consisting ... synthase GMP synthase glutamine dependent carbamoyl phosphate synthase phosphoribosylformylglycinamidine ... more details
6 3 1 2 GO code 0004356 image MN MN ADP PPQ.png width caption Active site between two monomers of glutamine ... site of glutamine synthetase illuminates the mechanism of enzymatic inhibition journal Biochemistry ... url issn ref Pfam box Symbol Gln synt N Name Glutamine synthetase, br beta Grasp domain image width 150 caption Crystallographic structure of glutamine synthetase from salmonella typhimurium . ref name ... 2qc8 , PDB2 2ojw Pfam box Symbol Gln synt C Name Glutamine synthetase, br catalytic domain image PDB 2gls EBI.jpg width caption 12 subunit enzyme glutamine synthetase from Salmonella typhimurium . ref ... D title Refined atomic model of glutamine synthetase at 3.5 A resolution journal J. Biol. Chem ... , PDB2 2ojw protein Name glutamate ammonia ligase glutamine synthetase caption image width HGNCid ... ECnumber 6.3.1.2 Chromosome 1 Arm q Band 31 LocusSupplementaryData stack end Glutamine synthetase ... catalysts glutamine synthetase and RuBisCO journal Cold Spring Harb. Symp. Quant. Biol. volume 52 issue ... in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine Glutamate Adenosine triphosphate ATP NH sub 3 sub Glutamine Adenosine diphosphate ADP phosphate Image GS reacction.PNG center alt Glutamine Synthetase reaction. Glutamine Synthetase Catalyzed Reaction. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration ... of the ammonium substrate site on glutamine synthetase, a third cation binding site journal Protein ... url issn ref The amide group of glutamate is a nitrogen source for the synthesis of glutamine ... Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine ... of ammonium ion, influences glutamine synthesis and glutamine hydrolysis. Glutamine is formed ... GM, Rotstein SH title Structure function relationships of glutamine synthetases journal Biochim Biophys ... model for the reaction mechanism of glutamine synthetase, based on five crystal structures ... more details
enzyme Name glutamine N phenylacetyltransferase EC number 2.3.1.14 CAS number 9030 00 6 IUBMB EC number 2 3 1 14 GO code 0047947 image width caption In enzymology , a glutamine N phenylacetyltransferase EC number 2.3.1.14 is an enzyme that catalysis catalyzes the chemical reaction phenylacetyl CoA L glutamine math rightleftharpoons math CoA alpha N phenylacetyl L glutamine Thus, the two substrate biochemistry substrates of this enzyme are phenylacetyl CoA and L glutamine , whereas its two product chemistry products are coenzyme A CoA and alpha N phenylacetyl L glutamine . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is phenylacetyl CoA L glutamine alpha N phenylacetyltransferase . Other names in common use include glutamine phenylacetyltransferase , and phenylacetyl CoA L glutamine N acetyltransferase . This enzyme participates in tyrosine metabolism and phenylalanine metabolism . References reflist 1 cite journal author Moldave K and Meister A year 1957 title Synthesis of phenylacetylglutamine by human tissue journal J. Biol. Chem. volume 229 pages 463&ndash 476 pmid 13491597 issue 1 Category EC 2.3.1 Category Enzymes of unknown structure transferase stub it Glutammina N fenilacetiltransferasi ... more details
enzyme Name glutamine scyllo inositol transaminase EC number 2.6.1.50 CAS number 9033 03 8 IUBMB EC number 2 6 1 50 GO code 0047310 image width caption In enzymology , a glutamine scyllo inositol transaminase EC number 2.6.1.50 is an enzyme that catalysis catalyzes the chemical reaction L glutamine 2,4,6 3,5 pentahydroxycyclohexanone math rightleftharpoons math 2 oxoglutaramate 1 amino 1 deoxy scyllo inositol Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and 2,4,6 3,5 pentahydroxycyclohexanone , whereas its two product chemistry products are 2 oxoglutaramate and 1 amino 1 deoxy scyllo inositol . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine 2,4,6 3,5 pentahydroxycyclohexanone aminotransferase . Other names in common use include glutamine scyllo inosose aminotransferase , L glutamine keto scyllo inositol aminotransferase , glutamine scyllo inosose transaminase , and L glutamine scyllo inosose transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Walker JB, Walker MS date 1969 title Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines journal Biochemistry. volume 8 pages 763&ndash 70 pmid 5781017 doi 10.1021 bi00831a003 issue 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name glutamine N acyltransferase EC number 2.3.1.68 CAS number 9030 00 6 IUBMB EC number 2 3 1 68 GO code 0047946 image width caption In enzymology , a glutamine N acyltransferase EC number 2.3.1.68 is an enzyme that catalysis catalyzes the chemical reaction acyl CoA L glutamine math rightleftharpoons math CoA N acyl L glutamine Thus, the two substrate biochemistry substrates of this enzyme are acyl CoA and L glutamine , whereas its two product chemistry products are coenzyme A CoA and N acyl L glutamine . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl CoA L glutamine N acyltransferase . References reflist 1 cite journal author Webster LT, Siddiqui UA, Lucas SV, Strong JM, Mieyal JJ date 1976 title Identification of separate acyl CoA glycine and acyl CoA L glutamine N acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man journal J. Biol. Chem. volume 251 pages 3352&ndash 8 pmid 931988 issue 11 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Glutammina N aciltransferasi ... more details
enzyme Name glutamine phenylpyruvate transaminase EC number 2.6.1.64 CAS number 68518 06 9 IUBMB EC number 2 6 1 64 GO code 0047316 image width caption In enzymology , a glutamine phenylpyruvate transaminase EC number 2.6.1.64 is an enzyme that catalysis catalyzes the chemical reaction L glutamine phenylpyruvate math rightleftharpoons math 2 oxoglutaramate L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and phenylpyruvate , whereas its two product chemistry products are 2 oxoglutaramate and L phenylalanine . This enzyme belongs to the family of transferase s, to be specific, the transaminases , that transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine phenylpyruvate aminotransferase . Other names in common use include glutamine transaminase K , and glutamine phenylpyruvate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1YIY and PDB link 1YIZ . References reflist 1 cite journal author Cooper AJ date 1978 title Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L phenylalanine and alpha keto gamma methiolbutyrate journal Anal. Biochem. volume 89 pages 451&ndash 60 pmid 727444 doi 10.1016 0003 2697 78 90374 3 issue 2 cite journal author Cooper AJ, Meister A date 1974 title Isolation and properties of a new glutamine transaminase from rat kidney journal J. Biol. Chem. volume 249 pages 2554&ndash 61 pmid 4822504 issue 8 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name glutamine pyruvate transaminase EC number 2.6.1.15 CAS number 9030 44 8 IUBMB EC number 2 6 1 15 GO code 0047945 image width caption In enzymology , a glutamine pyruvate transaminase EC number 2.6.1.15 is an enzyme that catalysis catalyzes the chemical reaction L glutamine pyruvate math rightleftharpoons math 2 oxoglutaramate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and pyruvate , whereas its two product chemistry products are 2 oxoglutaramate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine pyruvate aminotransferase . Other names in common use include glutaminase II , L glutamine transaminase L , and glutamine oxo acid transaminase . This enzyme participates in glutamate metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1V2D , PDB link 1V2E , and PDB link 1V2F . References reflist 1 cite journal author Cooper JL, Meister A date 1972 title Isolation and properties of highly purified glutamine transaminase journal Biochemistry. volume 11 pages 661&ndash 71 pmid 5059882 doi 10.1021 bi00755a001 issue 5 cite journal author MEISTER A date 1954 title Studies on the mechanism and specificity of the glutamine alpha keto acid transamination deamidation reaction journal J. Biol. Chem. volume 210 pages 17&ndash 35 pmid 13201566 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name protein glutamine glutaminase EC number 3.5.1.44 CAS number 62213 11 0 IUBMB EC number 3 5 1 44 GO code 0050568 image width caption In enzymology , a protein glutamine glutaminase EC number 3.5.1.44 is an enzyme that catalysis catalyzes the chemical reaction protein L glutamine H sub 2 sub O math rightleftharpoons math protein L glutamate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are protein L glutamine and water H sub 2 sub O , whereas its two product chemistry products are protein L glutamate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is protein L glutamine amidohydrolase . Other names in common use include peptidoglutaminase II , glutaminyl peptide glutaminase , destabilase , and peptidylglutaminase II . References reflist 1 cite journal author Kikuchi M, Hayashida H, Nakano E, Sakaguchi K date 1971 title Peptidoglutaminase. Enzymes for selective deamidation of gamma amide of peptide bound glutamine journal Biochemistry. volume 10 pages 1222&ndash 9 pmid 4928623 doi 10.1021 bi00783a019 issue 7 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
In biochemistry , the glutamate glutamine cycle is a sequence of events by which an adequate supply of the neurotransmitter glutamate is maintained in the central nervous system . ref name Purves cite book author Purves, Dale, George J. Augustine, David Fitzpatrick, William C. Hall, Anthony Samuel LaMantia, James O. McNamara, and Leonard E. White title Neuroscience. 4th ed. publisher Sinauer Associates pages 128 9 year 2008 isbn 978 0 87893 697 7 ref Initially, glial cell s release glutamine , which is then taken up into presynaptic terminal s and metabolized into glutamate by glutaminase a mitochondria l enzyme . Glutamate can also be produced by transamination of 2 oxoglutarate , an intermediate in the Citric acid cycle . ref name Purves The glutamate that is synthesized in the presynaptic terminal is packaged into synaptic vesicle s by the transporter VGLUT . Once the vesicle is released, glutamate is removed from the synaptic cleft by excitatory amino acid transporter s EAATs , of which there are five types. Glutamate taken up by glial cells is then converted into glutamine by glutamine synthetase , and transported out of the cells into the nerve terminal. This allows synaptic terminals and glial cells to work together in order to maintain a proper supply of glutamate. ref name Purves At GABAergic synapses, the cycle is called the GABA glutamine cycle. Here the glutamine taken up by neurons is converted to glutamate, which is then metabolized into GABA by glutamate decarboxylase . Upon release, GABA is taken up by glial cells via GABA transporters , metabolized into succinate, then in a series of steps to alpha ketoglutarate and then back to glutamine via glutamate. ref cite journal author Bak LK, Schousboe A, Waagepetersen HS title The glutamate GABA glutamine cycle aspects of transport, neurotransmitter homeostasis and ammonia transfer journal J. Neurochem. volume 98 issue 3 pages 641 53 year 2006 month August pmid 16787421 doi 10.1111 j.1471 4159.2006.03913.x ... more details
Orphan date February 2009 Glutamine oxoglutarate aminotransferase also known as Glutamate synthase is an enzyme and frequently abbreviated as GOGAT . This enzyme manufactures glutamate from glutamine and ketoglutarate , and thus along with glutamine synthetase abbreviated GS plays a central role in the regulation of Nitrogen fixation nitrogen assimilation in photosynthetic eukaryotes and prokaryotes. ref name Zadykowicz Phylogenetic Relationships Among Glutamate Synthase GOGAT Enzymes Eva Zadykowicz and Deborah L. Robertson Department of Biology, Clark University, Worcester, MA ref ref name Keiser Practical Streptomyces Genetics Keiser et al John Innes Foundation, Norwich, England ref This is of great importance as primary productivity in many marine environments is regulated by the availability of inorganic nitrogen. The primary sources of inorganic nitrogen used by marine algae are nitrate and ammonium . Both forms are ultimately incorporated into amino acids through the sequential reaction of glutamine synthetase GS and glutamate synthase glutamine 2 oxyoglutarate aminotransferase GOGAT . GOGAT isoenzymes catalyze the transfer of the amido nitrogen of glutamine to 2 oxoglutarate using pyridine nucleotides NADH NADPH dependent or ferredoxin Fd dependent as reductants. ref name Zadykowicz In photosynthetic eukaryotes, GS and GOGAT isoenzymes are localized in the cytosol and chloroplast . Fd GOGAT is found strictly in cyanobacteria and photosynthetic eukaryotes, and the gene is located in the chloroplast of rhodophytes and in the nucleus of vascular plants, but in both cases its product is active in the chloroplast. NADH GOGAT is found in the nucleus of vascular plants, fungi, and diatoms, while NADPH GOGAT is found in non photosynthetic bacteria and archaea. ref name Zadykowicz References reflist DEFAULTSORT Glutamine Oxoglutarate Aminotransferase Category Enzymes cell biology stub ... more details
enzyme Name glutamine tRNA ligase EC number 6.1.1.18 CAS number 9075 59 6 IUBMB EC number 6 1 1 18 GO code 0004819 image width caption In enzymology , a glutamine tRNA ligase EC number 6.1.1.18 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamine tRNAGln math rightleftharpoons math AMP diphosphate L glutaminyl tRNAGln The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamine , and tRNA Gln , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L glutaminyl tRNA Gln . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L glutamine tRNAGln ligase AMP forming . Other names in common use include glutaminyl tRNA synthetase , glutaminyl transfer RNA synthetase , glutaminyl transfer ribonucleate synthetase , glutamine tRNA synthetase , glutamine translase , glutamate tRNA ligase , glutaminyl ribonucleic acid , and GlnRS . This enzyme participates in glutamate metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 15 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EUQ , PDB link 1EUY , PDB link 1EXD , PDB link 1GSG , PDB link 1GTR , PDB link 1GTS , PDB link 1NYL , PDB link 1O0B , PDB link 1O0C , PDB link 1QRS , PDB link 1QRT , PDB link 1QRU , PDB link 1QTQ , PDB link 1ZJW , and PDB link 2HZ7 . References reflist 1 cite journal author Ravel JM, Wang S, Heinemeyer C and Shive W year 1965 title Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia coli W. Separation, properties, and stimulation of adenosine triphosphate pyrophosphate exchange by acceptor ribonucleic acid journal J. Biol. Chem. volume 240 pages 432&ndash 438 pmid 14253448 Ligases Category EC 6.1.1 Category Enzymes of known structure ligase stub ... more details
enzyme Name NAD synthase glutamine hydrolyzing EC number 6.3.5.1 CAS number 37318 70 0 IUBMB EC number 6 3 5 1 GO code 0003952 image width caption In enzymology , a NAD synthase glutamine hydrolysing EC number 6.3.5.1 is an enzyme that catalysis catalyzes the chemical reaction ATP deamido NAD sup sup L glutamine H sub 2 sub O math rightleftharpoons math AMP diphosphate NAD sup sup L glutamate The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , deamido NAD , L glutamine , and water H sub 2 sub O , whereas its 4 product chemistry products are adenosine monophosphate AMP , diphosphate , nicotinamide adenine dinucleotide NAD sup sup , and L glutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds carbon nitrogen ligases with glutamine as amido N donor. The systematic name of this enzyme class is deamido NAD L glutamine amido ligase AMP forming . Other names in common use include NAD synthetase glutamine hydrolysing , nicotinamide adenine dinucleotide synthetase glutamine , desamidonicotinamide adenine dinucleotide amidotransferase , and DPN synthetase . This enzyme participates in glutamate metabolism and nicotinate and nicotinamide metabolism . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EE1 , PDB link 1FYD , PDB link 1IFX , PDB link 1IH8 , PDB link 1KQP , PDB link 1NSY , and PDB link 2NSY . References reflist 1 cite journal author IMSANDE J date 1961 title Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli journal J. Biol. Chem. volume 236 pages 1494&ndash 7 pmid 13717628 cite journal author IMSANDE J, HANDLER P date 1961 title Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid mononucleotide pyrophos phorylase journal J. Biol. Chem. volume 236 pages 525&ndash 30 pmid 13717627 ligase stub Category EC 6.3.5 Category NADH dependent ... more details
enzyme Name glutamine fructose 6 phosphate transaminase isomerizing EC number 2.6.1.16 CAS number 9030 45 9 IUBMB EC number 2 6 1 16 GO code 0004360 image width caption In enzymology , a glutamine fructose 6 phosphate transaminase isomerizing EC number 2.6.1.16 is an enzyme that catalysis catalyzes the chemical reaction L glutamine D fructose 6 phosphate math rightleftharpoons math L glutamate D glucosamine 6 phosphate Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and D fructose 6 phosphate , whereas its two product chemistry products are L glutamate and D glucosamine 6 phosphate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine D fructose 6 phosphate isomerase deaminating . Other names in common use include hexosephosphate aminotransferase , glucosamine 6 phosphate isomerase glutamine forming , glutamine fructose 6 phosphate transaminase isomerizing , D fructose 6 phosphate amidotransferase , glucosaminephosphate isomerase , glucosamine 6 phosphate synthase , and GlcN6P synthase . This enzyme participates in glutamate metabolism and aminosugars metabolism . Structural studies As of late 2007, 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1JXA , PDB link 1MOQ , PDB link 1MOR , PDB link 1MOS , PDB link 1XFF , PDB link 1XFG , PDB link 2BPL , PDB link 2J6H , PDB link 2POC , PDB link 2PUT , PDB link 2PUV , and PDB link 2PUW . References reflist 1 cite journal author Ghosh S, Blumenthal HJ, Davidson E and Roseman S year 1960 title Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6 phosphate journal J. Biol. Chem. volume 235 pages 1265&ndash 1273 pmid 13827775 cite journal author GRYDER RM, POGELL BM year 1960 title Further studies on glucosamine 6 phosphate synthesis by rat liver enzymes journal J. Biol. Chem. volume 235 ... more details
OrganicBox complete wiki name Glutamine name 2S 2 amino 4 carbamoyl butanoic acid GENERAL INFORMATION C 5 H 10 N 2 O 3 mass 146.15 abbreviation Q, Gln image Image L glutamine skeletal.png 190px Chemical structure of Glutamine br Image L glutamine 3D sticks.png 205px Chemical structure of the amino acid glutamine synonyms D L Glutamine br 2 amino 4 carbamoylbutanoic acid br L D 2 aminoglutaramic acid br AI3 32686 br C00303 br Cebrogen br G107 br Glumin br Glutamic acid 5 amide br L D glutamid br Miglu P br NSC 97925 br NSC27421 DATABASES SMILES NC O CCC N C O O InChI 1 C5H10N2O3 c6 3 5 9 10 1 2 4 7 8 h3H,1 2,6H2, H2,7,8 H,9,10 f h9H,7H2 ATC prefix ATC suffix ATC supplemental CAS 56 85 9 DrugBank EINECS 200 292 1 PubChem br 738 ref 1 a , 145815 D ref 2 a , 5961 L ref 3 a PHYSICAL PROPERTIES Structure index of refraction abbe number dielectric constant magnetic susceptibility dipole moment U V data lambda max extinction coefficient Infrared data absorption bands NMR data proton NMR carbon NMR other NMR Spectrometry data mass spectrometry Phase behaviour delta fus H o delta fus S o delta vap H o delta vap S o triple point K triple point C triple point Pa criticle point K criticle point C criticle point Pa Solid properties delta f H o solid S o solid heat capacity solid density solid melting point C 185 melting point F melting point K Liquid properties delta f H o liquid S o liquid heat capacity liquid density liquid viscosity liquid boiling point C boiling point F boiling point K Gas properties delta f H o gas S o gas heat capacity gas viscosity gas HAZARD PROPERTIES MSDS main hazards nfpa health nfpa flammability nfpa reactivity nfpa special flash point r phrases s phrases RTECS number CHEMICAL PROPERTIES XLogP 4.102 isoelectric point 5.65 disociation constant 2.18 9.00 tautomers 2 H bond donor 3 H bond acceptor 4 PHARMACOLOGICAL PROPERTIES bioavailability metabolism elimination half life excretion pregnancy category legal status routes of administration References ... more details
enzyme Name protein glutamine gamma glutamyltransferase EC number 2.3.2.13 CAS number 80146 85 6 IUBMB EC number 2 3 2 13 GO code 0003810 image width caption Orphan date February 2009 In enzymology , a protein glutamine gamma glutamyltransferase EC number 2.3.2.13 is an enzyme that catalysis catalyzes the chemical reaction protein glutamine alkylamine math rightleftharpoons math protein N sub 5 sub alkylglutamine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are protein glutamine and Amine Aliphatic amines alkylamine , whereas its two product chemistry products are protein N 5 alkylglutamine and ammonia NH sub 3 sub . This enzyme participates in complement system complement and coagulation cascade s and Huntington s disease . It employs one cofactor biochemistry cofactor , calcium . Nomenclature This enzyme belongs to the family of transferase s, specifically the aminoacyltransferases . The systematic name of this enzyme class is protein glutamine amine gamma glutamyltransferase . Other names in common use include div col colwidth 30em factor XIIIa, fibrin stabilizing factor, fibrinoligase, glutaminylpeptide gamma glutamyltransferase, polyamine transglutaminase, R glutaminyl peptide amine gamma glutamyl transferase tissue transglutaminase, and transglutaminase. Div col end Structural studies As of late 2007, 19 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EVU , PDB link 1EX0 , PDB link 1F13 , PDB link 1FIE , PDB link 1G0D , PDB link 1GGT , PDB link 1GGU , PDB link 1GGY , PDB link 1IU4 , PDB link 1KV3 , PDB link 1L9M , PDB link 1L9N , PDB link 1NUD , PDB link 1NUF , PDB link 1NUG , PDB link 1QRK , PDB link 1RLE , PDB link 1SGX , and PDB link 1VJJ . References reflist 1 refbegin cite journal author Folk JE, Chung SI date 1973 title Molecular and catalytic properties of transglutaminases journal Adv. Enzymol. Relat. Areas. Mol. Biol. volume 38 pages 109&ndash ... more details
enzyme Name adenosylcobyric acid synthase glutamine hydrolyzing EC number 6.3.5.10 CAS number IUBMB EC number 6 3 5 10 GO code 0051921 image width caption In enzymology , an adenosylcobyric acid synthase glutamine hydrolysing EC number 6.3.5.10 is an enzyme that catalysis catalyzes the chemical reaction 4 ATP adenosylcobyrinic acid a,c diamide 4 L glutamine 4 H sub 2 sub O math rightleftharpoons math 4 ADP 4 phosphate adenosylcobyric acid 4 L glutamate The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , adenosylcobyrinic acid a,c diamide , L glutamine , and water H sub 2 sub O , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , adenosylcobyric acid , and L glutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds carbon nitrogen ligases with glutamine as amido N donor. The systematic name of this enzyme class is adenosylcobyrinic acid a,c diamide L glutamine amido ligase ADP forming . Other names in common use include CobQ , cobyric acid synthase , 5 deoxy 5 adenosylcobyrinic acid a,c diamide L glutamine , amido ligase , and Ado cobyric acid synthase glutamine hydrolyzing . This enzyme participates in porphyrin and chlorophyll metabolism . References reflist 1 cite journal author Blanche F, Couder M, Debussche L, Thibaut D, Cameron B, Crouzet J date 1991 title Biosynthesis of vitamin B12 stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c diamide is catalyzed by one enzyme in Pseudomonas denitrificans journal J. Bacteriol. volume 173 pages 6046&ndash 51 pmid 1917839 issue 19 pmc 208350 cite journal author Warren MJ, Raux E, Schubert HL, Escalante Semerena JC date 2002 title The biosynthesis of adenosylcobalamin vitamin B12 journal Nat. Prod. Rep. volume 19 pages 390&ndash 412 pmid 12195810 doi 10.1039 b108967f issue 4 ligase stub Category EC 6.3.5 Category Enzymes of unknown structure ... more details
enzyme Name asparaginyl tRNA synthase glutamine hydrolyzing EC number 6.3.5.6 CAS number 37211 76 0 IUBMB EC number 6 3 5 6 GO code 0050566 image width caption In enzymology , an asparaginyl tRNA synthase glutamine hydrolysing EC number 6.3.5.6 is an enzyme that catalysis catalyzes the chemical reaction ATP aspartyl tRNAAsn L glutamine math rightleftharpoons math ADP phosphate asparaginyl tRNAAsn L glutamate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , aspartyl tRNA Asn , and L glutamine , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , asparaginyl tRNA Asn , and L glutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds carbon nitrogen ligases with glutamine as amido N donor. The systematic name of this enzyme class is aspartyl tRNAAsn L glutamine amido ligase ADP forming . Other names in common use include Asp AdT , Asp tRNAAsn amidotransferase , aspartyl tRNAAsn amidotransferase , and Asn tRNAAsn L glutamine amido ligase ADP forming . This enzyme participates in glutamate metabolism and alanine and aspartate metabolism . References reflist 1 cite journal author Min B, Pelaschier JT, Graham DE, Tumbula Hansen D, Soll D date 2002 title Transfer RNA dependent amino acid biosynthesis an essential route to asparagine formation journal Proc. Natl. Acad. Sci. U. S. A. volume 99 pages 2678&ndash 83 pmid 11880622 doi 10.1073 pnas.012027399 issue 5 pmc 122407 cite journal author Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D date 1998 title Glutamyl tRNA Gln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis journal Proc. Natl. Acad. Sci. U. S. A. volume 95 pages 12838&ndash 43 pmid 9789001 doi 10.1073 pnas.95.22.12838 issue 22 pmc 23620 cite journal author Ibba M, Soll D date 2000 title Aminoacyl tRNA synthesis journal Annu. Rev. Biochem. volume 69 issue 1 pages 617&ndash 50 pmid 10966471 doi 10.1146 annurev.biochem.69.1.617 ... more details
enzyme Name glutaminyl tRNA synthase glutamine hydrolyzing EC number 6.3.5.7 CAS number 52232 48 1 IUBMB EC number 6 3 5 7 GO code 0050567 image width caption In enzymology , a glutaminyl tRNA synthase glutamine hydrolysing EC number 6.3.5.7 is an enzyme that catalysis catalyzes the chemical reaction ATP glutamyl tRNAGln L glutamine math rightleftharpoons math ADP phosphate glutaminyl tRNAGln L glutamate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , glutamyl tRNA Gln , and L glutamine , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , glutaminyl tRNA Gln , and L glutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds carbon nitrogen ligases with glutamine as amido N donor. The systematic name of this enzyme class is glutamyl tRNAGln L glutamine amido ligase ADP forming . Other names in common use include Glu AdT , Glu tRNAGln amidotransferase , glutamyl tRNAGln amidotransferase , and Glu tRNAGln L glutamine amido ligase ADP forming . This enzyme participates in glutamate metabolism and alanine and aspartate metabolism . References reflist 1 cite journal author Horiuchi KY, Harpel MR, Shen L, Luo Y, Rogers KC, Copeland RA date 2001 title Mechanistic studies of reaction coupling in Glu tRNAGln amidotransferase journal Biochemistry. volume 40 pages 6450&ndash 7 pmid 11371208 doi 10.1021 bi002599l issue 21 cite journal author Curnow AW, Tumbula DL, Pelaschier JT, Min B, Soll D date 1998 title Glutamyl tRNA Gln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis journal Proc. Natl. Acad. Sci. U. S. A. volume 95 pages 12838&ndash 43 pmid 9789001 doi 10.1073 pnas.95.22.12838 issue 22 pmc 23620 cite journal author Ibba M, Soll D date 2000 title Aminoacyl tRNA synthesis journal Annu. Rev. Biochem. volume 69 pages 617&ndash 50 pmid 10966471 doi 10.1146 annurev.biochem.69.1.617 ligase stub Category EC 6.3.5 Category ... more details
enzyme Name hydrogenobyrinic acid a,c diamide synthase glutamine hydrolysing EC number 6.3.5.9 CAS number 132053 22 6 IUBMB EC number 6 3 5 9 GO code 0043802 image width caption In enzymology , a hydrogenobyrinic acid a,c diamide synthase glutamine hydrolysing EC number 6.3.5.9 is an enzyme that catalysis catalyzes the chemical reaction 2 ATP hydrogenobyrinic acid 2 L glutamine 2 H sub 2 sub O math rightleftharpoons math 2 ADP 2 phosphate hydrogenobyrinic acid a,c diamide 2 L glutamate The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , hydrogenobyrinic acid , L glutamine , and water H sub 2 sub O , whereas its 4 product chemistry products are adenosine diphosphate ADP , phosphate , hydrogenobyrinic acid a,c diamide , and L glutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds carbon nitrogen ligases with glutamine as amido N donor. The systematic name of this enzyme class is hydrogenobyrinic acid L glutamine amido ligase AMP forming . This enzyme is also called CobB . This enzyme participates in porphyrin and chlorophyll metabolism . References reflist 1 cite journal author Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F date 1990 title Purification and characterization of cobyrinic acid a,c diamide synthase from Pseudomonas denitrificans journal J. Bacteriol. volume 172 pages 6239&ndash 44 pmid 2172209 issue 11 pmc 526805 cite journal author Warren MJ, Raux E, Schubert HL, Escalante Semerena JC date 2002 title The biosynthesis of adenosylcobalamin vitamin B12 journal Nat. Prod. Rep. volume 19 pages 390&ndash 412 pmid 12195810 doi 10.1039 b108967f issue 4 ligase stub Category EC 6.3.5 Category Enzymes of unknown structure ... more details
enzyme Name D glutamyltransferase EC number 2.3.2.1 CAS number 9030 02 8 IUBMB EC number 2 3 2 1 GO code 0047823 image width caption In enzymology , a D glutamyltransferase EC number 2.3.2.1 is an enzyme that catalysis catalyzes the chemical reaction L or D glutamine D glutamyl peptide math rightleftharpoons math NH sub 3 sub 5 glutamyl D glutamyl peptide The 3 substrate biochemistry substrates of this enzyme are L glutamine , D glutamine , and D glutamyl peptide , whereas its two product chemistry products are ammonia NH sub 3 sub and 5 glutamyl D glutamyl peptide . This enzyme belongs to the family of transferase s, specifically the aminoacyltransferase s. The systematic name of this enzyme class is glutamine D glutamyl peptide 5 glutamyltransferase . Other names in common use include D glutamyl transpeptidase , and D gamma glutamyl transpeptidase . This enzyme participates in d glutamine and d glutamate metabolism . References reflist 1 cite journal author Williams WJ, Litwin J and Thorne CB date 1955 title Further studies on the biosynthesis of gamma glutamyl peptides by transfer reactions journal J. Biol. Chem. volume 212 pages 427&ndash 438 transferase stub Category EC 2.3.2 Category Enzymes of unknown structure it D glutammiltransferasi ... more details
Adenylylation ref name pmid1582530 ref name Garrett is a posttranslational modification that can occur to molecules such as tyrosine residues. Adenylylation involves a phosphodiester bond between a hydroxyl group of the molecule undergoing adenylylation and the phosphate group of the adenosine monophosphate nucleotide i.e. adenylic acid . The degree of adenylylation depends on the ratio of glutamine to ketoglutarate The higher this ratio the more monomers are adenylylated, thereby producing lower activity of glutamine synthetase the lower the ratio the less monomers are adenylated and the higher activity of glutamine synthetase. A high ratio is a sign of cellular nitrogen sufficiency, whereas a low ratio is evidence of a limited nitrogen and the need for ammonia fixation by glutamine synthetase. References Reflist refs ref name Garrett Garrett, R.H., and C.M. Grisham. Biochemistry. 3rd ed. Belmont, CA Thomas, 2007. 815 20 ref ref name pmid1582530 cite journal author Han KK, Martinage A title Post translational chemical modification s of proteins journal Int. J. Biochem. volume 24 issue 1 pages 19 28 year 1992 pmid 1582530 doi url ref Protein primary structure Category Biochemistry biochem stub ... more details
enzyme Name D glutaminase EC number 3.5.1.35 CAS number 37289 12 6 IUBMB EC number 3 5 1 35 GO code 0050001 image width caption In enzymology , a D glutaminase EC number 3.5.1.35 is an enzyme that catalysis catalyzes the chemical reaction D glutamine H sub 2 sub O math rightleftharpoons math D glutamate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are D glutamine and water H sub 2 sub O , whereas its two product chemistry products are D glutamate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is D glutamine amidohydrolase . This enzyme participates in d glutamine and d glutamate metabolism and nitrogen metabolism . References reflist 1 cite journal author Domnas A and Catimo EC date 1965 title The behavior of amidohydrolases and L glutamate in synchronized populations of Blastocladiella emeronii journal Phytochemistry journal Phytochemistry volume 4 pages 273&ndash 284 doi 10.1016 S0031 9422 00 86173 7 issue 2 Category EC 3.5.1 Category Enzymes of unknown structure hydrolase stub ... more details
enzyme Name peptidyl glutaminase EC number 3.5.1.43 CAS number 37228 70 9 IUBMB EC number 3 5 1 43 GO code 0050170 image width caption In enzymology , a peptidyl glutaminase EC number 3.5.1.43 is an enzyme that catalysis catalyzes the chemical reaction alpha N peptidyl L glutamine H sub 2 sub O math rightleftharpoons math alpha N peptidyl L glutamate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are alpha N peptidyl L glutamine and water H sub 2 sub O , whereas its two product chemistry products are alpha N peptidyl L glutamate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is peptidyl L glutamine amidohydrolase . Other names in common use include peptidoglutaminase I , peptideglutaminase , and peptidoglutaminase . References reflist 1 cite journal author Kikuchi M, Hayashida H, Nakano E, Sakaguchi K date 1971 title Peptidoglutaminase. Enzymes for selective deamidation of gamma amide of peptide bound glutamine journal Biochemistry. volume 10 pages 1222&ndash 9 pmid 4928623 doi 10.1021 bi00783a019 issue 7 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name theanine hydrolase EC number 3.5.1.65 CAS number 99533 51 4 IUBMB EC number 3 5 1 65 GO code 0050330 image width caption In enzymology , a theanine hydrolase EC number 3.5.1.65 is an enzyme that catalysis catalyzes the chemical reaction N sub 5 sub ethyl L glutamine H sub 2 sub O math rightleftharpoons math L glutamate ethylamine Thus, the two substrate biochemistry substrates of this enzyme are N5 ethyl L glutamine and water H sub 2 sub O , whereas its two product chemistry products are L glutamate and ethylamine . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N5 ethyl L glutamine amidohydrolase . Other names in common use include L theanine amidohydrolase , and 5 N ethyl L glutamine amidohydrolase . References reflist 1 cite journal author Tsushida T and Takeo T date 1985 title An enzyme hydrolyzing L theanine in tea leaves journal Agric. Biol. Chem. volume 49 pages 2913&ndash 2917 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name adenylyl glutamate ammonia ligase hydrolase EC number 3.1.4.15 CAS number 37288 22 5 IUBMB EC number 3 1 4 15 GO code 0047388 image width caption In enzymology , an adenylyl glutamate ammonia ligase hydrolase EC number 3.1.4.15 is an enzyme that catalysis catalyzes the chemical reaction adenylyl L glutamate ammonia ligase ADP forming H sub 2 sub O math rightleftharpoons math adenylate L glutamate ammonia ligase ADP forming Thus, the two substrate biochemistry substrates of this enzyme are adenylyl L glutamate ammonia ligase ADP forming and water H sub 2 sub O , whereas its two product chemistry products are adenylate and L glutamate ammonia ligase ADP forming . This enzyme belongs to the family of hydrolase s, specifically those acting on phosphoric ester diester bonds. The systematic name of this enzyme class is adenylyl L glutamate ammonia ligase ADP forming adenylylhydrolase . Other names in common use include adenylyl glutamine synthetase hydrolase , and adenylyl glutamine synthetase hydrolase . References reflist 1 cite journal author Heilmeyer L, Battig F and Holzer H date 1968 title Characterization of a glutamine synthetase b activating deadenylylating enzyme system in Escherichia coli journal Eur. J. Biochem. volume 9 pages 259&ndash 262 doi 10.1111 j.1432 1033.1969.tb00603.x pmid 4897098 cite journal author Shapiro BM date 1969 title The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements journal Biochemistry. volume 8 pages 659&ndash 70 pmid 4893578 doi 10.1021 bi00830a030 issue 2 cite journal author Shapiro BM, Stadtman ER date 1968 title 5 adenylyl O tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli journal J. Biol. Chem. volume 243 pages 3769&ndash 71 pmid 4298074 issue 13 hydrolase stub Category EC 3.1.4 Category Enzymes of unknown structure ... more details
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