about general ligases DNA specific ligases DNA ligase In biochemistry , ligase from the Latin language Latin verb lig re &mdash to bind or to glue together is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond , usually with accompanying hydrolysis of a small chemical group dependent to one of the larger molecules or the enzyme catalyzing the linking together of two compounds....e.g. Enzymes which catalyze joining of C O,C S,C N etc. .In general, a ligase catalyzes the following reaction Ab C A&ndash C b or sometimes Ab cD A&ndash D b c where the lowercase letters signify the small, dependent groups. Nomenclature The common names of ligase enzymes often include the word ligase, such as DNA ligase , an enzyme commonly used in molecular biology laboratory laboratories to join together DNA fragments. Other common names for ligases include synthetases , because they are used to Biosynthesis synthesize new molecules. Note that, originally, biochemical nomenclature distinguished synthetases and synthase s. Under the original definition, synthases do not use energy from nucleoside triphosphates such as ATP, GTP, CTP, TTP, and UTP , whereas synthetases do use nucleoside triphosphates. It is also said that a synthase is a lyase a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure and does not require any energy, whereas a synthetase is a ligase a ligase is an enzyme that binds two chemicals or compounds and thus requires energy. However, the Joint Commission on Biochemical Nomenclature JCBN dictates that synthase can ... EC 6.6 EC 6.6 includes ligases used to form nitrogen metal bonds See also DNA ligase References references ... Ligase de Ligase es Ligasa fr Ligase gl Ligase id Ligase it Ligasi he kk lt Ligaz s nl Ligase ja no Ligase pl Ligazy pt Ligase ru fi Ligaasi sv Ligas tr Ligaz uk ur ... more details
Refimprove date February 2007 enzyme Name DNA ligase EC number 6.5.1.1 CAS number 9015 85 4 IUBMB EC number 6 5 1 1 GO code 0003910 image DNA Repair.jpg width caption DNA ligase repairing chromosomal damage protein Name ligase I, DNA, ATP dependent caption image DNA Ligase.jpg width 200 HGNCid 6598 Symbol ... 19 Arm Band LocusSupplementaryData protein Name ligase III, DNA, ATP dependent caption image width ... PDB ECnumber Chromosome 17 Arm q Band 11.2 LocusSupplementaryData q12 protein Name ligase IV, DNA, ATP ... biology , DNA ligase is a specific type of enzyme, a ligase , EC number 6.5.1.1 that repairs ... double strand break a break in both complementary strands of DNA . Purified DNA ligase is used in gene ... type of DNA ligase using the Complementary DNA complementary strand as a template, ref name pmid15565146 cite journal pages 473 8 doi 10.1038 nature03082 title Human DNA ligase I completely encircles ... 7016 pmid 15565146 ref but still requires DNA ligase to create the final phosphodiester bond to fully repair the DNA. DNA ligase has applications in both DNA repair and DNA replication see DNA ligase Mammalian ligases Mammalian ligases . In addition, DNA ligase has extensive use in molecular biology laboratories for Genetic recombination experiments see DNA ligase Applications in molecular biology research Applications in molecular biology research . Ligase mechanism The mechanism of DNA ligase ... with the 5 end 5 phosphate end of another donor . ATP is required for the ligase reaction, which ... science.186.4166.790 title DNA Ligase Structure, Mechanism, and Function year 1974 last1 Lehnman first1 ... 2 A pictorial example of how a ligase works with DNA end sticky end s Ligase will also work with DNA .... Mammalian ligases This section is linked from DNA ligase In mammals, there are four specific types of ligase. LIG1 DNA ligase I ligates the nascent DNA of the Replication fork Lagging strand lagging strand after the Ribonuclease H has removed the RNA primer from the Okazaki fragment s. DNA ligase ... more details
Image Class I Ligase Ribozyme.jpg thumb Crystal structure of the Class I ligase ribozyme at 2.98 resolution PDB ID http www.rcsb.org pdb explore explore.do?structureId 3HHN 3HHN . The phosphodiester bond formed by this enzyme is shown as spheres. Image Figure 2d.200.jpg The L1 Ligase Ribozyme 2.6 crystal structure right thumb 200px The RNA Ligase ribozyme was the first of several types of Ribozyme Synthetic ribozymes synthetic ribozymes produced by in vitro evolution and selection techniques. They are an important class of ribozymes because they catalyze the assembly of RNA fragments into phosphodiester RNA polymers, a reaction required of all extant nucleic acid polymerases and thought to be required for any self replicating molecule. Ideas that the origin of life may have involved the first self replicating molecules being ribozymes are called RNA World RNA World hypotheses . Ligase ribozymes may have been part of such a pre biotic RNA world. In order to copy RNA, fragments or monomers individual building blocks that have Nucleotide 5 triphosphates must be ligated together. This is true for modern protein based Rna Polymerase polymerases , and is also the most likely mechanism by which a ribozyme self replicase in an RNA world might function. Yet no one has found a natural ribozyme ... group has even produced a functional RNA polymerase ribozyme. The L1 ligase Michael Robertson and Andrew Ellington evolved a ligase ribozyme that performs the desired Phosphodiester bonds 5 3 RNA assembly reaction, and called this the L1 ligase. ref name pmid11345430 cite journal author Robertson MP, Hesselberth JR, Ellington AD title Optimization and optimality of a short ribozyme ligase that joins ... MP, Scott WG, York DM title Identification of dynamical hinge points of the L1 ligase molecular ... title Structure guided engineering of the regioselectivity of RNA ligase ribozymes journal J. Am. Chem ... Ligase Ribozyme Category Non coding RNA Category Ribozymes Category RNA splicing ... more details
enzyme Name Ubiquitin protein ligase EC number 6.3.2.19 CAS number 74812 49 0 IUBMB EC number 6 3 2 19 GO code 0051444 image 4a4c.png width caption E3 ubiquitin ligase Cbl blue in complex with E2 cyan and substrate peptide green . PDB entry PDBe 4a4c ref cite pmid 22266821 ref A ubiquitin ligase also called an E3 ubiquitin ligase is a protein that in combination with an E2 ubiquitin conjugating enzyme causes the attachment of ubiquitin to a lysine on a target protein via an isopeptide bond the E3 ubiquitin ligase targets specific protein substrates for degradation by the proteasome . In general, the ubiquitin ligase is involved in polyubiquitination A second ubiquitin is attached to the first, a third is attached to the second, and so forth. Polyubiquitination marks proteins for degradation by the proteasome. However, there are some ubiquitination events that are limited to mono ubiquitination, in which only a single ubiquitin is added by the ubiquitin ligase to a substrate molecule. Mono ubiquitinated proteins are not targeted to the proteasome for degradation, but may instead be altered ..., among other functions. Overview In enzymology , an ubiquitin protein ligase EC number 6.3.2.19 ... belongs to the family of ligase s, to be specific those forming carbon nitrogen bonds as acid ... protein lysine N ligase AMP forming . This enzyme is also called ubiquitin activating enzyme . This enzyme ... system The ubiquitin ligase is referred to as an E3, and operates in conjunction with an ubiquitin ... system. gallery Ubiquitin ligase families The anaphase promoting complex APC and the SCF complex Skp1 Cullin F box protein complex are two examples of ubiquitin ligase protein scaffold involved in recognition ... been discovered to fall into specific groups called ubiquitin ligase families. Examples A RING finger .... Individual E3 ubiquitin ligases Ubiquitin protein ligase E3A E3A mdm2 Anaphase promoting complex ... Ligase Category EC 6.3 Category Posttranslational modification ru zh ... more details
Infobox protein family Symbol Mur ligase Name Mur ligase image width caption Pfam PF01225 Pfam clan CL0063 InterPro IPR000713 SMART PROSITE PDOC00773 MEROPS SCOP 1uag TCDB OPM family 415 OPM protein 1p31 CAZy CDD The bacteria bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall Virus structure shape of the cell biology cell . The Base chemistry basic peptidoglycan structure of both Gram positive and Gram negative Zinc dependent phospholipase C bacteria comprises a sheet of glycan chains connected by short cross linking polypeptides . Biosynthesis of peptidoglycan is a multi step 11 12 steps process comprising three main stages 1 formation of UDP N acetylmuramic acid UDPMurNAc from N acetylglucosamine GlcNAc . 2 addition of a short polypeptide chain to the UDPMurNAc. 3 addition of a second GlcNAc to the disaccharide pentapeptide building block and transport of this unit through the cytoplasmic membrane and incorporation into the growing peptidoglycan layer. Stage two involves four key Mur ubiquitin ligase enzymes MurC http expasy.org enzyme 6.3.2.8 EC , ref name pmid17139082 cite journal author Deva T, Baker EN, Squire CJ, Smith CA title Structure of Escherichia coli UDP N acetylmuramoyl L alanine ligase MurC journal Acta Crystallogr. D Biol. Crystallogr. volume 62 issue Pt 12 pages 1466 74 year 2006 month December pmid 17139082 doi 10.1107 S0907444906038376 url ref MurD http expasy.org enzyme 6.3.2.9 EC , ref ... motif sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family ... terminal domain of several stage 2 Mur ligases, including UDP N acetylmuramate L alanine ligase MurC , UDP N acetylmuramoylalanyl D glutamate 2,6 diaminopimelate ligase MurE , and UDP N acetylmuramoyl tripeptide D alanyl D alanine ligase MurF . This entry also includes folylpolyglutamate synthase ... more details
and parkin itself see also ubiquitin ligase . Additionally, Parkin contains a C terminus C terminal ... Parkin ligase has been shown to Protein protein interaction interact with STUB1 , ref name ... its ubiquitin ligase activity journal Mol. Cell volume 10 issue 1 pages 55 67 publisher location ... month Mar. title Parkin is a component of an SCF like ubiquitin ligase complex and protects postmitotic ... de Ubiquitin Protein Ligase Parkin ... more details
enzyme Name 4 Coumarate CoA ligase EC number 6.2.1.12 CAS number 37332 51 7 IUBMB EC number 6 2 1 12 GO code 0016207 image width caption In enzymology , a 4 coumarate CoA ligase EC number 6.2.1.12 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 coumarate CoA math rightleftharpoons math AMP diphosphate 4 coumaroyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 4 coumarate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 4 coumaroyl CoA . This enzyme belongs to the family of ligase s, to be specific those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 4 coumarate CoA ligase AMP forming . Other names in common use include 4 coumaroyl CoA synthetase , p coumaroyl CoA ligase , p coumaryl coenzyme A synthetase , p coumaryl CoA synthetase , p coumaryl CoA ligase , feruloyl CoA ligase , hydroxycinnamoyl CoA synthetase , 4 coumarate coenzyme A ligase , caffeolyl coenzyme A synthetase , p hydroxycinnamoyl coenzyme A synthetase , feruloyl coenzyme A synthetase , sinapoyl coenzyme A synthetase , 4 coumaryl CoA synthetase , hydroxycinnamate CoA ligase , p coumaryl CoA ligase , p hydroxycinnamic acid CoA ligase , and 4CL . This enzyme participates in phenylpropanoid biosynthesis . References reflist 1 cite journal author Gross GG, Zenk MH date 1974 title Isolation and properties of hydroxycinnamate CoA ligase from lignifying tissue of Forsythia journal Eur. J. Biochem. volume 42 pages 453 9 pmid 4364250 doi 10.1111 j.1432 1033.1974.tb03359.x issue 2 cite journal author Lindl T, Kreuzaler F, Hahlbrock K date 1973 title Synthesis of p coumaroyl coenzyme a with a partially purified p coumarate CoA ligase from cell ... pmid 4699252 issue 2 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure fr 4 coumarate CoA ligase ... more details
enzyme Name phenylacetate CoA ligase EC number 6.2.1.30 CAS number 57219 71 3 IUBMB EC number 6 2 1 30 GO code 0047475 image width caption In enzymology , a phenylacetate CoA ligase is an enzyme that catalysis catalyzes the chemical reaction ATP phenylacetate CoA math rightleftharpoons math AMP diphosphate phenylacetyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , phenylacetic acid phenylacetate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and phenylacetyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is phenylacetate CoA ligase AMP forming . Other names in common use include phenylacetyl CoA ligase , PA CoA ligase , and phenylacetyl CoA ligase AMP forming . This enzyme participates in tyrosine metabolism and phenylalanine metabolism . References reflist 1 cite journal author Martinez Blanco H, Reglero A, Rodriguez Aparicio LB, Luengo JM date 1990 title Purification and biochemical characterization of phenylacetyl CoA ligase from Pseudomonas putida. A specific enzyme for the catabolism of phenylacetic acid journal J. Biol. Chem. volume 265 pages 7084&ndash 90 pmid 2324116 issue 12 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name anthranilate CoA ligase EC number 6.2.1.32 CAS number 112692 58 7 IUBMB EC number 6 2 1 32 GO code 0018860 image width caption In enzymology , an anthranilate CoA ligase EC number 6.2.1.32 is an enzyme that catalysis catalyzes the chemical reaction ATP anthranilate CoA math rightleftharpoons math AMP diphosphate anthranilyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , anthranilate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and anthranilyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is anthranilate CoA ligase AMP forming . Other names in common use include anthraniloyl coenzyme A synthetase , 2 aminobenzoate CoA ligase , 2 aminobenzoate coenzyme A ligase , and 2 aminobenzoate coenzyme A ligase . This enzyme participates in 3 metabolism metabolic pathways carbazole degradation , benzoate degradation via coa ligation , and acridone alkaloid biosynthesis . References reflist 1 cite journal author Altenschmidt U, Eckerskorn C, Fuchs G date 1990 title Evidence that enzymes of a novel aerobic 2 amino benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid journal Eur. J. Biochem. volume 194 pages 647&ndash 53 pmid 2176602 doi 10.1111 j.1432 1033.1990.tb15664.x issue 2 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name 4 hydroxybenzoate CoA ligase EC number 6.2.1.27 CAS number 119699 80 8 IUBMB EC number 6 2 1 27 GO code 0018859 image width caption In enzymology , a 4 hydroxybenzoate CoA ligase EC number 6.2.1.27 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 hydroxybenzoate CoA math rightleftharpoons math AMP diphosphate 4 hydroxybenzoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 4 hydroxybenzoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 4 hydroxybenzoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 4 hydroxybenzoate CoA ligase AMP forming . Other names in common use include 4 hydroxybenzoate CoA synthetase , 4 hydroxybenzoate coenzyme A ligase AMP forming , 4 hydroxybenzoyl coenzyme A synthetase , and 4 hydroxybenzoyl CoA ligase . This enzyme participates in benzoate degradation via coa ligation . References reflist 1 cite journal author Merkel SM, Eberhard AE, Gibson J, Harwood CS date 1989 title Involvement of coenzyme A thioesters in anaerobic metabolism of 4 hydroxybenzoate by Rhodopseudomonas palustris journal J. Bacteriol. volume 171 pages 1&ndash 7 pmid 2914844 issue 1 pmc 209545 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name phytanate CoA ligase EC number 6.2.1.24 CAS number 105238 50 4 IUBMB EC number 6 2 1 24 GO code 0050197 image width caption In enzymology , a phytanate CoA ligase EC number 6.2.1.24 is an enzyme that catalysis catalyzes the chemical reaction ATP phytanate CoA math rightleftharpoons math AMP diphosphate phytanoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , phytanate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and phytanoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is phytanate CoA ligase AMP forming . This enzyme is also called phytanoyl CoA ligase . References reflist 1 cite journal author Muralidharan FN, Muralidharan VB date 1986 title Phytanoyl CoA ligase activity in rat liver journal Biochem. Int. volume 13 pages 123&ndash 30 pmid 3753503 issue 1 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name RNA ligase ATP EC number 6.5.1.3 CAS number 37353 39 2 IUBMB EC number 6 5 1 3 GO code 0003972 image width caption In enzymology , an RNA ligase ATP EC number 6.5.1.3 is an enzyme that catalysis catalyzes the chemical reaction ATP ribonucleotide n ribonucleotide m math rightleftharpoons math AMP diphosphate ribonucleotide n sup sup m The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , ribonucleotide n , and ribonucleotide m , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and ribonucleotide n m . This enzyme belongs to the family of ligase s, specifically those forming phosphoric ester bonds. The systematic name of this enzyme class is poly ribonucleotide poly ribonucleotide ligase AMP forming . Other names in common use include polyribonucleotide synthase ATP , RNA ligase , polyribonucleotide ligase , and ribonucleic ligase . 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 1VDX and PDB link 2C5U . References reflist 1 cite journal author Silber R, Malathi VG, Hurwitz J date 1972 title Purification and properties of bacteriophage T4 induced RNA ligase journal Proc. Natl. Acad. Sci. U.S.A. volume 69 pages 3009&ndash 13 pmid 4342972 doi 10.1073 pnas.69.10.3009 issue 10 pmc 389696 ligase stub Category EC 6.5.1 Category Enzymes of known structure ... more details
enzyme Name citrate pro 3S lyase ligase EC number 6.2.1.22 CAS number 52660 22 7 IUBMB EC number 6 2 1 22 GO code 0008771 image width caption In enzymology , a citrate pro 3S lyase ligase EC number 6.2.1.22 is an enzyme that catalysis catalyzes the chemical reaction ATP acetate citrate pro 3S lyase thiol form math rightleftharpoons math AMP diphosphate citrate pro 3S lyase acetyl form The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , acetate , and citrate pro 3S lyase thiol form , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and citrate pro 3S lyase acetyl form . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is acetate citrate pro 3S lyase thiol form ligase AMP forming . Other names in common use include citrate lyase ligase , citrate lyase synthetase , acetate SH acyl carrier protein enzyme ligase AMP , acetate HS citrate lyase ligase , and acetate citrate pro 3S lyase thiol form ligase AMP forming . This enzyme participates in two component system general . References reflist 1 cite journal author Antranikian G, Gottschalk G date 1982 title Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes journal Eur. J. Biochem. volume 126 pages 43&ndash 7 pmid 7128585 doi 10.1111 j.1432 1033.1982.tb06743.x issue 1 cite journal author Antranikian G, Herzberg C, Gottschalk G date 1985 title Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation dephosphorylation journal Eur. J. Biochem. volume 153 pages 413&ndash 20 pmid 3935436 doi 10.1111 j.1432 1033.1985.tb09318.x issue 2 cite journal author Quentmeier A, Antranikian G date 1985 title Characterization of citrate lyase ... Pro 3s Lyase Ligase Category EC 6.2.1 Category Enzymes of unknown structure ligase stub ... more details
enzyme Name 2,3 dihydroxybenzoate serine ligase EC number 6.3.2.14 CAS number 37318 63 1 IUBMB EC number 6 3 2 14 GO code 0047527 image width caption In enzymology , a 2,3 dihydroxybenzoate serine ligase EC number 6.3.2.14 is an enzyme that catalysis catalyzes the chemical reaction ATP 2,3 dihydroxybenzoate L serine math rightleftharpoons math products of ATP breakdown N 2,3 dihydroxybenzoyl L serine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 2,3 dihydroxybenzoate , and L serine , whereas its two product chemistry products are products of ATP breakdown and N 2,3 dihydroxybenzoyl L serine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D amino acid ligases peptide synthases . The systematic name of this enzyme class is 2,3 dihydroxybenzoate L serine ligase . Other names in common use include N 2,3 dihydroxybenzoyl serine synthetase , and 2,3 dihydroxybenzoylserine synthetase . References reflist 1 cite journal author Brot N, Goodwin J date 1968 title Regulation of 2,3 dihydroxybenzoylserine synthetase by iron journal J. Biol. Chem. volume 243 pages 510&ndash 3 pmid 4966114 issue 3 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
enzyme Name 2 furoate CoA ligase EC number 6.2.1.31 CAS number 122320 08 5 IUBMB EC number 6 2 1 31 GO code 0047541 image width caption In enzymology , a 2 furoate CoA ligase EC number 6.2.1.31 is an enzyme that catalysis catalyzes the chemical reaction ATP 2 furoate CoA math rightleftharpoons math AMP diphosphate 2 furoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 2 furoate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 2 furoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is 2 furoate CoA ligase AMP forming . This enzyme is also called 2 furoyl coenzyme A synthetase . References reflist 1 cite journal author Koenig K, Andreesen JR date 1989 title Molybdenum Involvement in Aerobic Degradation of 2 Furoic Acid by Pseudomonas putida Fu1 journal Appl. Environ. Microbiol. volume 55 pages 1829&ndash 1834 pmid 16347977 issue 7 pmc 202958 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name 4 methyleneglutamate ammonia ligase EC number 6.3.1.7 CAS number 85537 85 5 IUBMB EC number 6 3 1 7 GO code 0047581 image width caption In enzymology , a 4 methyleneglutamate ammonia ligase EC number 6.3.1.7 is an enzyme that catalysis catalyzes the chemical reaction ATP 4 methylene L glutamate NH sub 3 sub math rightleftharpoons math AMP diphosphate 4 methylene L glutamine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , 4 methylene L glutamate , and ammonia NH sub 3 sub , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and 4 methylene L glutamine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is 4 methylene L glutamate ammonia ligase AMP forming . This enzyme is also called 4 methyleneglutamine synthetase . This enzyme participates in c5 branched dibasic acid metabolism . References reflist 1 cite journal author Winter HC, Su TZ, Dekker EE date 1983 title 4 methyleneglutamine synthetase a new amide synthetase present in germinating peanuts journal Biochem. Biophys. Res. Commun. volume 111 pages 484&ndash 9 pmid 6838571 doi 10.1016 0006 291X 83 90332 7 issue 2 ligase stub Category EC 6.3.1 Category Enzymes of unknown structure ... more details
enzyme Name 5 formyltetrahydrofolate cyclo ligase EC number 6.3.3.2 CAS number 37318 64 2 IUBMB EC number 6 3 3 2 GO code 0030272 image width caption In enzymology , a 5 formyltetrahydrofolate cyclo ligase EC number 6.3.3.2 is an enzyme that catalysis catalyzes the chemical reaction ATP 5 formyltetrahydrofolate math rightleftharpoons math ADP phosphate 5,10 methenyltetrahydrofolate Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and 5 formyltetrahydrofolate , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and 5,10 methenyltetrahydrofolate . This enzyme belongs to the family of ligase s, specifically the cyclo ligases, which form carbon nitrogen bonds. The systematic name of this enzyme class is 5 formyltetrahydrofolate cyclo ligase ADP forming . Other names in common use include 5,10 methenyltetrahydrofolate synthetase , formyltetrahydrofolic cyclodehydrase , and 5 formyltetrahydrofolate cyclodehydrase . This enzyme participates in one carbon pool by folate . Structural studies As of late 2007, 5 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1SBQ , PDB link 1SOU , PDB link 1U3F , PDB link 1U3G , and PDB link 2JCB . References reflist 1 cite journal author Greenberg DM, Wynston LK and Nagabhushanan A date 1965 title Further studies on N5 formyltetrahydrofolic acid cyclodehydrase journal Biochemistry volume 4 pages 1872&ndash 1878 doi 10.1021 bi00885a026 issue 9 ligase stub Category EC 6.3.3 Category Enzymes of known structure ... more details
enzyme Name acetoacetate CoA ligase EC number 6.2.1.16 CAS number 39394 62 2 IUBMB EC number 6 2 1 16 GO code 0030729 image width caption In enzymology , an acetoacetate CoA ligase EC number 6.2.1.16 is an enzyme that catalysis catalyzes the chemical reaction ATP acetoacetate CoA math rightleftharpoons math AMP diphosphate acetoacetyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , acetoacetate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and acetoacetyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is acetoacetate CoA ligase AMP forming . This enzyme is also called acetoacetyl CoA synthetase . This enzyme participates in butanoate metabolism . References reflist 1 cite journal author Fukui T, Ito M, Tomita K date 1982 title Purification and characterization of acetoacetyl CoA synthetase from Zoogloea ramigera I 16 M journal Eur. J. Biochem. volume 127 pages 423&ndash 8 pmid 7140777 doi 10.1111 j.1432 1033.1982.tb06889.x issue 2 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name arachidonate CoA ligase EC number 6.2.1.15 CAS number 82047 87 8 IUBMB EC number 6 2 1 15 GO code 0047676 image width caption In enzymology , an arachidonate CoA ligase EC number 6.2.1.15 is an enzyme that catalysis catalyzes the chemical reaction ATP arachidonate CoA math rightleftharpoons math AMP diphosphate arachidonoyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , arachidonate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and arachidonoyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is arachidonate CoA ligase AMP forming . This enzyme is also called arachidonoyl CoA synthetase . References reflist 1 cite journal author Wilson DB, Prescott SM, Majerus PW date 1982 title Discovery of an arachidonoyl coenzyme A synthetase in human platelets journal J. Biol. Chem. volume 257 pages 3510&ndash 5 pmid 7061494 issue 7 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name biotin CoA ligase EC number 6.2.1.11 CAS number 37318 60 8 IUBMB EC number 6 2 1 11 GO code 0047707 image width caption In enzymology , a biotin CoA ligase EC number 6.2.1.11 is an enzyme that catalysis catalyzes the chemical reaction ATP biotin CoA math rightleftharpoons math AMP diphosphate biotinyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , biotin , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and biotinyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is biotin CoA ligase AMP forming . Other names in common use include biotinyl CoA synthetase , biotin CoA synthetase , and biotinyl coenzyme A synthetase . This enzyme participates in biotin metabolism . References reflist 1 cite journal author CHRISTNER JE, SCHLESINGER MJ, COON MJ date 1964 title ENZYMATIC ACTIVATION OF BIOTIN. BIOTINYL ADENYLATE FORMATION journal J. Biol. Chem. volume 239 pages 3997&ndash 4005 pmid 14257635 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name dicarboxylate CoA ligase EC number 6.2.1.23 CAS number 99332 77 1 IUBMB EC number 6 2 1 23 GO code 0047851 image width caption In enzymology , a dicarboxylate CoA ligase EC number 6.2.1.23 is an enzyme that catalysis catalyzes the chemical reaction ATP an alphaomega dicarboxylic acid CoA math rightleftharpoons math AMP diphosphate an omega carboxyacyl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , alphaomega dicarboxylic acid , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and omega carboxyacyl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is omega dicarboxylate CoA ligase AMP forming . Other names in common use include carboxylyl CoA synthetase , and dicarboxylyl CoA synthetase . References reflist 1 cite journal author Vamecq J, de Hoffmann E, Van Hoof F date 1985 title The microsomal dicarboxylyl CoA synthetase journal Biochem. J. volume 230 pages 683&ndash 93 pmid 4062873 issue 3 pmc 1152672 ligase stub Category EC 6.2.1 Category Enzymes of unknown structure ... more details
enzyme Name formate dihydrofolate ligase EC number 6.3.4.17 CAS number 123303 25 3 IUBMB EC number 6 3 4 17 GO code 0047897 image width caption In enzymology , a formate dihydrofolate ligase EC number 6.3.4.17 is an enzyme that catalysis catalyzes the chemical reaction ATP formate dihydrofolate math rightleftharpoons math ADP phosphate 10 formyldihydrofolate The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , formate , and dihydrofolate , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and 10 formyldihydrofolate . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is formate dihydrofolate ligase ADP forming . Other names in common use include formyltransferase, dihydrofolate , dihydrofolate formyltransferase , and formyl dihydrofolate synthase . References reflist 1 Further reading refbegin cite journal author Drake JC, Baram J, Allegra CJ date 1990 title Isolation and characterization of a novel dihydrofolate formylating enzyme from human MCF 7 breast cancer cells journal Biochem. Pharmacol. volume 39 pages 615&ndash 8 pmid 2306274 doi 10.1016 0006 2952 90 90073 T issue 3 refend ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name glutamate methylamine ligase EC number 6.3.4.12 CAS number 37318 69 7 IUBMB EC number 6 3 4 12 GO code 0047943 image width caption In enzymology , a glutamate methylamine ligase EC number 6.3.4.12 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate methylamine math rightleftharpoons math ADP phosphate N sub 5 sub methyl L glutamine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and methylamine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and N5 methyl L glutamine . This enzyme belongs to the family of ligase s, specifically those forming generic carbon nitrogen bonds. The systematic name of this enzyme class is L glutamate methylamine ligase ADP forming . This enzyme is also called gamma glutamylmethylamide synthetase . References reflist 1 cite journal author Kung HF, Wagner C date 1969 title Gamma glutamylmethylamide. A new intermediate in the metabolism of methylamine journal J. Biol. Chem. volume 244 pages 4136&ndash 40 pmid 5800436 issue 15 ligase stub Category EC 6.3.4 Category Enzymes of unknown structure ... more details
enzyme Name Glutamate putrescine ligase EC number 6.3.1.11 CAS number 914090 78 1 IUBMB EC number 6 3 1 11 GO code image width caption In enzymology , a glutamate putrescine ligase EC number 6.3.1.11 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamate putrescine math rightleftharpoons math ADP phosphate gamma L glutamylputrescine The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamate , and putrescine , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and gamma L glutamylputrescine . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds as acid D ammonia or amine ligases amide synthases . The systematic name of this enzyme class is L glutamate putrescine ligase ADP forming . Other names in common use include gamma glutamylputrescine synthetase , and YcjK . This enzyme participates in urea cycle and metabolism of amino groups . References reflist 1 cite journal author Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H date 2005 title A novel putrescine utilization pathway involves gamma glutamylated intermediates of Escherichia coli K 12 journal J. Biol. Chem. volume 280 pages 4602&ndash 8 pmid 15590624 doi 10.1074 jbc.M411114200 issue 6 ligase stub Category EC 6.3.1 Category Enzymes of unknown structure ... more details
enzyme Name glutarate CoA ligase EC number 6.2.1.6 CAS number 9023 68 1 IUBMB EC number 6 2 1 6 GO code 0047948 image width caption In enzymology , a glutarate CoA ligase EC number 6.2.1.6 is an enzyme that catalysis catalyzes the chemical reaction ATP glutarate CoA math rightleftharpoons math ADP phosphate glutaryl CoA The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , glutarate , and coenzyme A CoA , whereas its 3 product chemistry products are adenosine diphosphate ADP , phosphate , and glutaryl CoA . This enzyme belongs to the family of ligase s, specifically those forming carbon sulfur bonds as acid thiol ligases. The systematic name of this enzyme class is glutarate CoA ligase ADP forming . Other names in common use include glutaryl CoA synthetase , and glutaryl coenzyme A synthetase . This enzyme participates in fatty acid metabolism and lysine degradation . References reflist 1 cite journal author Menon GKK, Friedman DL and Stern JR year 1960 title Enzymic synthesis of glutaryl coenzyme A journal Biochim. Biophys. Acta volume 44 pages 375&ndash 377 doi 10.1016 0006 3002 60 91583 3 pmid 13769477 Category EC 6.2.1 Category Enzymes of unknown structure ligase stub ... more details
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