enzyme Name 3 hydroxyisobutyryl CoA hydrolase EC number 3.1.2.4 CAS number 9025 88 1 IUBMB EC number 3 1 2 4 GO code 0003860 image width caption In enzymology , a 3 hydroxyisobutyryl CoA hydrolase EC number 3.1.2.4 is an enzyme that catalysis catalyzes the chemical reaction 3 hydroxy 2 methylpropanoyl CoA H sub 2 sub O math rightleftharpoons math CoA 3 hydroxy 2 methylpropanoate Thus, the two substrate biochemistry substrates of this enzyme are 3 hydroxy 2 methylpropanoyl CoA and water H sub 2 sub O , whereas its two product chemistry products are coenzyme A CoA and 3 hydroxy 2 methylpropanoate . This enzyme belongs to the family of hydrolase s, specifically those acting on thioester bonds. The systematic name of this enzyme class is 3 hydroxy 2 methylpropanoyl CoA hydrolase . Other names in common use include 3 hydroxy isobutyryl CoA hydrolase , and HIB CoA deacylase . This enzyme participates in 3 metabolism metabolic pathways valine, leucine and isoleucine degradation , beta alanine metabolism , and propanoate metabolism . References reflist 1 cite journal author Rendina G and Coon MJ year 1957 title Enzymatic hydrolysis of the coenzyme A thiol esters of beta hydroxypropionic and beta hydroxyisobutyric acids journal J. Biol. Chem. volume 225 issue 1 pages 523&ndash 534 pmid 13457352 Category EC 3.1.2 Category Enzymes of unknown structure hydrolase stub ... more details
enzyme Name valine pyruvate transaminase EC number 2.6.1.66 CAS number 132421 38 6 IUBMB EC number 2 6 1 66 GO code 0009042 image width caption In enzymology , a valine pyruvate transaminase EC number 2.6.1.66 is an enzyme that catalysis catalyzes the chemical reaction L valine pyruvate math rightleftharpoons math 3 methyl 2 oxobutanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L valine and pyruvate , whereas its two product chemistry products are 3 methyl 2 oxobutanoate 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 valine pyruvate aminotransferase . Other names in common use include transaminase C , valine pyruvate aminotransferase , and alanine oxoisovalerate aminotransferase . This enzyme participates in valine, leucine and isoleucine biosynthesis . References reflist 1 cite journal author Falkinham JO 3rd date 1979 title Identification of a mutation affecting an alanine alpha ketoisovalerate transaminase activity in Escherichia coli K 12 journal Mol. Gen. Genet. volume 176 pages 147&ndash 9 pmid 396446 doi 10.1007 BF00334306 issue 1 cite journal author RUDMAN D, MEISTER A date 1953 title Transamination in Escherichia coli journal J. Biol. Chem. volume 200 pages 591&ndash 604 pmid 13034817 issue 2 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
refimprove date February 2008 Leucine responsive protein , or Lrp , ref name pmid17223133 cite journal author de los Rios S, Perona JJ title Structure of the Escherichia coli leucine responsive regulatory protein Lrp reveals a novel octameric assembly journal J. Mol. Biol. volume 366 issue 5 pages 1589 602 year 2007 month March pmid 17223133 pmc 1933502 doi 10.1016 j.jmb.2006.12.032 url http linkinghub.elsevier.com retrieve pii S0022 2836 06 01707 4 ref is a global regulator protein , meaning that it regulates the biosynthesis of leucine , as well as the other branched chain amino acids , valine and isoleucine . In bacteria , it is encoded by the lrp gene . Lrp alternatively activates and represses the expression of acetolactate synthase s ALS several isoenzymes . Lrp, in E. coli, along with Dam methylase DAM plays a role in the regulation of the pap operon , pylonephritis associated pili . I m too lazy busy to look up refs for this, but you can find most of them from the article Metabolic engineering of E coli for the production of valine based on transcriptome analysis and in silico gene knockout simulation by Park et al., 2007 References reflist External links MeshName Leucine Responsive Regulatory Protein Category Proteins biochemistry stub ... more details
chembox verifiedrevid 434223591 ImageFile 2,3 Dihydroxy 3 methylpentanoic acid.png ImageSize 180px IUPACName 2,3 dihydroxy 3 methylpentanoic acid OtherNames Section1 Chembox Identifiers ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 7 KEGG Ref keggcite correct kegg KEGG C04104 InChI 1 C6H12O4 c1 3 6 2,10 4 7 5 8 9 h4,7,10H,3H2,1 2H3, H,8,9 InChIKey PDGXJDXVGMHUIR UHFFFAOYAA SMILES1 O C O C O C O C CC StdInChI Ref stdinchicite correct chemspider StdInChI 1S C6H12O4 c1 3 6 2,10 4 7 5 8 9 h4,7,10H,3H2,1 2H3, H,8,9 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey PDGXJDXVGMHUIR UHFFFAOYSA N CASNo 562 43 6 PubChem 8 SMILES CCC C C C O O O O MeSHName 2,3 dihydroxy 3 methylpentanoic acid Section2 Chembox Properties Formula C sub 6 sub H sub 12 sub O sub 4 sub MolarMass 148.16 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition 2,3 Dihydroxy 3 methylpentanoic acid is an intermediate in the metabolism of isoleucine . Amino acid metabolism intermediates DEFAULTSORT Dihydoxy 3 methylpentanoic acid, 2,3 Category Hydroxy acids organic compound stub fr Acide 2,3 dihydroxy 3 m thylpentano que ... more details
chembox verifiedrevid 265864648 ImageFile tiglyl CoA.png ImageSize 250px IUPACName small S 2 3 nowiki nowiki 2 R 4 nowiki nowiki 2 R ,3 S ,4 R ,5 R 5 6 Aminopurin 9 yl 4 hydroxy 3 phosphonooxyoxolan 2 yl methoxy hydroxyphosphoryl oxy hydroxyphosphoryl oxy 2 hydroxy 3,3 dimethylbutanoyl amino propanoylamino ethyl E 2 methylbut 2 enethioate small OtherNames Section1 Chembox Identifiers CASNo 6247 62 7 PubChem 6443760 SMILES C C C C C O SCCNC O CCNC O C H C C C COP O O OP O O OC C H 1 C H C H C H O1 N2C NC3 C2N CN C3N O OP O O O O MeSHName tiglyl coenzyme A Section2 Chembox Properties Formula C sub 26 sub H sub 42 sub N sub 7 sub O sub 17 sub P sub 3 sub S MolarMass 849.63 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Tiglyl CoA is an intermediate in the metabolism of isoleucine . Amino acid metabolism intermediates Category Coenzymes organic compound stub fr Tiglyl coenzyme A ... more details
Drugbox verifiedrevid 422827080 IUPAC name image Ergocryptine.png width 250 drug name alpha Ergocryptine Clinical data tradename pregnancy category legal AU legal UK legal US routes of administration Pharmacokinetic data metabolism excretion Identifiers CAS number Ref cascite correct ?? CAS number 511 09 1 ATC prefix ATC suffix PubChem 134551 Chemical data C 32 H 41 N 5 O 5 molecular weight 575.698 g mol Ergocryptine is an ergopeptine and one of the ergot alkaloid s. It is often used in LSD synthesis, rather than ergotamine. Citation needed date March 2011 Chemistry Ergocryptine is a mixture of two very similar compounds, alpha and beta ergocryptine beta ergocryptine . ref cite doi 10.1021 jf00064a038 ref The beta differs from the alpha form only in the position of a single methyl group, which is a consequence of the biosynthesis in which the proteinogenic amino acid leucine is replaced by isoleucine . See also Dihydroergocryptine References reflist Ergolines Category Ergot alkaloids Category Lactams Category Oxazolopyrrolopyrazines nervous system drug stub eo Ergokriptino ... more details
Cytochrome P450 2C9 CYP2C9 , a member of the CYP2C enzyme subfamily, ranks amongst the most important drug metabolizing enzymes in humans. Human CYP2C9 has been shown to exhibit genetic Polymorphism biology polymorphism . In addition to the wild type protein CYP2C9 1, at least 32 single nucleotide polymorphisms SNPs have been reported within the coding region of the CYP2C9 gene producing the variant allozymes. ref name CYP2C9 http www.cypalleles.ki.se cyp2c9.htm CYP2C9 allele nomenclature ref CYP2C9 3 is one of them. CYP2C9 3 reflects an Isoleucine Ile 359 Leucine Leu I359L change in the amino acid sequence ref name CYP2C9 , and have reduced catalytic activity compared with the wild type CYP2C9 1 . ref Sullivan Klose TH, Ghanayem BI, Bell DA, Zhang ZY, Kaminsky LS, Shenfield GM, Miners JO, Birkett DJ, Goldstein JA, The role of the CYP2C9 Leu359 allelic variant in the tolbutamide polymorphism Pharmacogenetics. 1996 Aug 6 4 341 9 ref class wikitable border 1 colspan 6 Allele frequencies of CYP2C9 polymorphism African American Black African Pygmy Asian Caucasian CYP2C9 3 2.0 0 2.3 0 1.1 3.6 3.3 16.2 References references Category Enzymes Category Human proteins Category Cytochrome P450 gene 10 stub ... more details
be consumed in the diet, and so are called essential amino acids those are histidine , isoleucine ... small L small Histidine br His H image L isoleucine skeletal.png Isoleucine small L small Isoleucine br Ile I image L leucine skeletal.png Leucine small L small Leucine ... or aspartic acid Glx Z is glutamic acid or glutamine Xle J is leucine or isoleucine In addition ... G Gly 75.06714 6.06 2.35 9.78 Histidine H His 155.15634 7.60 1.80 9.33 Isoleucine I Ile 131.17464 ... H sub 3 sub N sub 2 sub 6.04 X weak basic Aromatic 118 Isoleucine I Ile CH CH sub 3 sub CH sub 2 sub ... Histidine H His CAU, CAC 2.3 Yes Isoleucine I Ile AUU, AUC, AUA 5.3 Yes Lysine K Lys AAA, AAG 5.9 ... sub H sub 7 sub N sub 3 sub O 137.05891 137.1411 Isoleucine I Ile C sub 6 sub H sub 11 sub NO 113.08406 ... acid 1.5 7 1 Phenylalanine 1.1 6 2 Glycine 3.5 2 2 Histidine 0.54 1 7 Isoleucine 1.7 7 11 Lysine 2.0 ... amino acids. Like isoleucine, leucine and valine, these are hydrophobic and tend to orient towards ... it is comparatively scarce. Isoleucine I Ile essential amino acid Essential for humans. Isoleucine ... tend to be located inside of the protein molecule. Leucine or isoleucine J Xle A placeholder ... Leu essential amino acid Essential for humans. Behaves similar to isoleucine and valine. See isoleucine ... amino acid Essential for humans. Behaves similarly to isoleucine and leucine. See isoleucine ... more details
Unreferenced stub auto yes date December 2009 A tripeptide is a peptide consisting of three amino acids joined by peptide bond s. Examples of tripeptides are Eisenin pGlu Gln Ala OH is a peptide with immunological activity that is isolated from the Japanese marine alga, Eisenia bicyclis , which more commonly is known as, Arame Copper peptide GHK Cu GHK Cu glycyl small L small histidyl small L small lysine is a human copper binding peptide with wound healing and skin remodeling activity, which is used in anti aging cosmetics and more commonly referred to as Copper peptide GHK Cu copper peptide Glutathione small L small Glutamyl small L small cysteinylglycine is an important antioxidant in animal cells Isoleucine proline proline IPP found in milk products, acts as an ACE inhibitor Leupeptin N acetyl small L small leucyl small L small leucyl small L small argininal is a Protease inhibitor biology protease inhibitor that also acts as an inhibitor of calpain Melanostatin prolyl leucyl glycinamide is a peptide hormone produced in the hypothalamus that inhibits the release of melanocyte stimulating hormone MSH Ophthalmic acid small L small glutamyl small L small aminobutyryl glycine is an analogue of glutathione isolated from lens anatomy crystalline lens Norophthalmic acid y glutamyl alanyl glycine is an analogue of glutathione small L small cysteine replaced by small L small alanine isolated from crystalline lens Thyrotropin releasing hormone TRH, thyroliberin or protirelin small L small pyroglutamyl small L small histidinyl small L small prolinamide is a peptide hormone that stimulates the release of thyroid stimulating hormone and prolactin by the anterior pituitary ACV small L small aminoadipyl small L small Cys small D small Val is a key precursor in penicillin and cephalosporin biosyntheses. See also Dipeptide Tetrapeptide Category Peptides Protein stub tr Tripeptid zh ... more details
The branched chain keto acid dehydrogenase complex is a combination of enzyme s responsible for the degradation of the branched chain amino acids . Examples of these include valine , isoleucine , and leucine . Cofactors This complex requires the following 5 cofactors Thiamine diphosphate FAD Nicotinamide adenine dinucleotide NAD sup sup Lipoic acid Lipoate Coenzyme A Similar enzymes This complex is also analogous to the alpha ketoglutarate dehydrogenase complex in the citric acid cycle and the pyruvate dehydrogenase complex creating acetyl CoA prior to the citric acid cycle. Pathology A deficiency in any of the enzymes of this complex as well as an enzyme inhibitor inhibition of the complex as a whole is responsible for maple syrup urine disease . This enzyme is an autoantigen recognized in primary biliary cirrhosis , a form of acute liver failure. These antibodies appear to recognize oxidized protein that has resulted from inflammatory immune responses. Some of these inflammatory responses are explained by gluten sensitivity . ref name pmid17657817 cite journal author Leung PS, Rossaro L, Davis PA, et al. title Antimitochondrial antibodies in acute liver failure Implications for primary biliary cirrhosis journal Hepatology volume 46 issue 5 pages 1436 year 2007 pmid 17657817 doi 10.1002 hep.21828 ref . Other mitochondrial autoantigens include pyruvate dehydrogenase and branched chain oxoglutarate dehydrogenase , which are antigens recognized by anti mitochondrial antibodies . References Reflist External links http www.ncbi.nlm.nih.gov bookshelf br.fcgi?book gene&part msud GeneReviews NCBI NIH UW entry on Maple Syrup Urine Disease MeshName Branched Chain Ketoacid Dehydrogenase EC number 1.2.4.4 Autoantigens Aldehyde Oxo oxidoreductases Amino acid metabolism enzymes Multienzyme complexes DEFAULTSORT Branched Chain Alpha Keto Acid Dehydrogenase Complex Category Autoantigens ... more details
Infobox disease Name 2 Methylbutyryl CoA dehydrogenase deficiency Image 2 Methylbutanoyl CoA.png Caption 2 Methylbutyryl CoA DiseasesDB 34413 ICD10 ICD9 ICDO OMIM 610006 MedlinePlus eMedicineSubj eMedicineTopic MeshID 2 Methylbutyryl CoA dehydrogenase deficiency , also called 2 Methylbutyryl glycinuria or short branched chain acyl CoA dehydrogenase deficiency SBCADD , ref name omim OMIM 610006 2 Methylbutyryl CoA dehydrogenase deficiency ref is an autosome autosomal dominance genetics recessive inborn errors of metabolism metabolic disorder . ref name aur07 cite pmid 17883863 ref It causes the body to be unable to process the amino acid isoleucine properly. Signs and symptoms Untreated SBCADD can lead to progressive loss of motor skills , mental retardation and epilepsy . Citation needed date April 2011 Cause and genetics Image Autorecessive.jpg thumb right 2 Methylbutyryl CoA dehydrogenase deficiency has an autosomal recessive pattern of inheritance. The disorder is caused by a mutation in the ACADSB gene , located on the long arm of human chromosome 10 human chromosome 10 10q25 q26 . ref name omim ref cite pmid 17945527 ref It is inherited in an autosomal recessive manner. ref name aur07 This means the defective gene responsible for the disorder is located on an autosome chromosome 10 is an autosome , and two copies of the defective gene one inherited from each parent are required in order to be born with the disorder. The parents of an individual with an autosomal recessive disorder both genetic carrier carry one copy of the defective gene, but usually do not experience any signs or symptoms of the disorder. References reflist External links http www.wadsworth.org newborn babhealth.htm Short descriptions of genetic disorders from wadsworth.org Amino acid metabolic pathology Category Amino acid metabolism disorders Category Autosomal recessive disorders Genetic disorder stub ... more details
There are three primary nutrient macronutrients defined as being the classes of chemical compounds humans consume in the largest quantities and which provide bulk energy. These are protein , fat , and carbohydrate . This list shows the categorizeation of the most common food components by these macronutrients. Macronutrients can also refer to the chemical elements humans consume in the largest quantities, see Nutrient . tocright Protein Amino acids Standard amino acids Alanine Arginine Aspartic acid Aspartic acid aspartate Asparagine Cystine Glutamic acid Glutamic acid glutamate Glutamine Glycine Histidine Isoleucine branched chain amino acid Leucine branched chain amino acid Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine branched chain amino acid Fat Saturated fats Butear assid Caprioc acid Caprylic acid Capric acid Lauric acid Myristic acid Pentadecanoic acid Palmitic acid Heptadec acid Stearic acid Arachidic acid Behenate acid Tetracos acid Compound acid Monounsaturated fats Myristol Pentadecenoic Palmitoyl Heptadecenoic Oleic acid Eicosen Erucic acid Nervonic acid Polyunsaturated fats Linoleic acid Linolenic acid Linolenic acid Stearidon Eicosatrienoic Arachidon eicosapentaenoic acid EPA an essential fatty acid DPA DHA docosahexaenoic acid an essential fatty acid Essential fatty acids eicosapentaenoic acid EPA DHA docosahexaenoic acid Other fats Omega 3 fatty acid Omega 3 fatty acid s Omega 6 fatty acid Omega 6 fatty acid s Trans fatty acids Cholesterol Carbohydrates Starches Sugars Fructose Galactose Glucose Lactose Maltose Sucrose See also List of micronutrients Category Medical lists Macronutrients vi Danh s ch ch t dinh d ng a l ng ... more details
protein Name complement component 1, q subcomponent, A chain caption image width HGNCid 1241 Symbol C1QA AltSymbols EntrezGene 712 OMIM 120550 RefSeq NM 015991 UniProt P02745 PDB ECnumber Chromosome 1 Arm p Band 36.3 LocusSupplementaryData 34.1 protein Name complement component 1, q subcomponent, B chain caption image width HGNCid 1242 Symbol C1QB AltSymbols EntrezGene 713 OMIM 120570 RefSeq NM 000491 UniProt P02746 PDB ECnumber Chromosome 1 Arm p Band 36.3 LocusSupplementaryData 34.1 protein Name complement component 1, q subcomponent, C chain caption image width HGNCid 1245 Symbol C1QC AltSymbols C1QG EntrezGene 714 OMIM 120575 RefSeq NM 172369 UniProt P02747 PDB ECnumber Chromosome 1 Arm p Band 36.11 LocusSupplementaryData The C1q complex is potentially multivalent for attachment to the complement fixation sites of immunoglobulin . The sites are on the CH2 domain of IgG and, it is thought, on the CH4 domain of IgM . The appropriate peptide sequence of the complement fixing site might become exposed following complexing of the immunoglobulin, or the sites might always be available, but might require multiple attachment by C1q with critical geometry in order to achieve the necessary avidity . Structure C1q is a 400kDa protein formed from 18 peptide chains in 3 subunits of 6. Each 6 peptide subunit consists of a Y shaped pair of triple peptide helices joined at the stem and ending in a globular non helical head. The 80 amino acid helical component of each triple peptide contain many Gly X Y sequences, where X and Y are proline , isoleucine , or hydroxylysine they, therefore, strongly resemble collagen fibrils . Function Image Complement pathway.png thumb 270px center The classical and alternative complement pathways. It is assumed that the globular ends are the sites for multivalent attachment to the complement fixing sites in immune complexed immunoglobulin. Patients suffering from Lupus erythematosus often have deficient expression of C1q. External links MeshName ... more details
An immunoreceptor tyrosine based activation motif ITAM in the antagonistic case immunoreceptor tyrosine based inhibitory motif ITIM , I for inhibition is a conserved sequence of four amino acid s that is repeated twice in the cytoplasmic tails of certain cell surface proteins of the immune system . ref name basic citation last1 Abbas first1 Abul K last2 Lichtman first2 Andrew H. title Basic Immunology Functions and Disorders of the Immune System year 2009 publisher Saunders edition 3 place Philadelphia, PA isbn 978 1 4160 4688 2 ref Structure The motif contains a tyrosine separated from a leucine or isoleucine by any two other amino acid s, giving the signature YxxL. ref name basic Two of these signatures are typically separated by between 7 and 12 amino acids in the tail of the molecule YxxLx sub 7 12 sub YxxL . Function Image TCRComplex.png thumb The T cell receptor complex with TCR and TCR chains, CD3 receptor CD3 and chain accessory molecules. ITAMs are represented in blue on the tails of the CD3 subunits. ITAMs are important for signal transduction in immune cells. Hence, they are found in the tails of important cell signaling molecules such as the CD3 receptor CD3 and chain s of the T cell receptor complex, ref name basic the CD79 alpha and beta chains of the B cell receptor complex, and certain Fc receptor s. The tyrosine residues within these motifs become phosphorylated following interaction of the receptor molecules with their ligand s and form docking sites for other proteins involved in the cell signaling signaling pathways of the cell. References reflist DEFAULTSORT Immunoreceptor Tyrosine Based Activation Motif Category Cell signaling Category Immune system Protein stub Immunology stub ... more details
enzyme for isoleucine and valine biosynthesis in Escherichia coli K 12 during growth on acetate as the sole ..., leucine, and isoleucine. All three of these amino acids are essential amino acids and cannot be synthesized ... to isoleucine and leucine valine does not affect it directly. Both the ilvGMEDA and ilvBNC operons are derepressed ... more details
protein Name short branched chain specific acyl CoA dehydrogenase caption Cartoon diagram of human short branched chain acyl CoA dehydrogenase in complex with FAD and Coenzyme A CoASH . Chloride ions visible as green spheres. From PDB 2JIF image Short branched chain acyl CoA dehydrogenase 2JIF.png width HGNCid 91 Symbol ACADSB AltSymbols EntrezGene 36 OMIM 600301 RefSeq NM 001609 UniProt P45954 PDB ECnumber 1.3.99.3 Chromosome 10 Arm q Band 25 LocusSupplementaryData q26 ACADSB is a human gene that encodes short branched chain specific acyl CoA dehydrogenase SBCAD , an enzyme in the acyl CoA dehydrogenase family. It can cause short branched chain acyl CoA dehydrogenase deficiency . ref name pmid11013134 cite journal author Andresen BS, Christensen E, Corydon TJ, et al title Isolated 2 methylbutyrylglycinuria caused by short branched chain acyl CoA dehydrogenase deficiency identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl CoA dehydrogenases in isoleucine and valine metabolism journal Am. J. Hum. Genet. volume 67 issue 5 pages 1095 103 year 2000 month November pmid 11013134 pmc 1288551 doi 10.1086 303105 url http linkinghub.elsevier.com retrieve pii S0002 9297 07 62939 5 ref References reflist oxidoreductase stub CH CH oxidoreductases Lipid metabolism enzymes Category EC 1.3.99 Category Genes on chromosome 10 ... more details
protein Name branched chain aminotransferase caption cite web url http www.rcsb.org pdb explore explore.do?structureId 3DTF title RCSB Protein Data Bank Structure Summary for 3DTF Structural analysis of mycobacterial branched chain aminotransferase implications for inhibitor design format work accessdate image Branched Chain Aminotransferase.png width HGNCid 977 Symbol BCAT AltSymbols BCT EntrezGene 587 OMIM 113530 RefSeq NM 001190 UniProt O15382 PDB ECnumber 2.6.1.42 Chromosome 19 Arm q Band 13 LocusSupplementaryData Branched chain aminotransferase is an aminotransferase enzyme which acts upon branched chain amino acids . It uses largely ketoglutarate in forming branched chain keto acids and glutamate . The structure to the right of branched chain aminotransferase was found using X ray diffraction with a resolution of 2.20 . The branched chain aminotransferase found in this image was isolated from mycobacteria . This protein is made up of two identical polypeptide chains . The protein is a total of 372 residues 1 . As can be seen in the image, the protein is made of helices and beta sheets. The biological function of branched chain aminotransferases is to catalyse the synthesis of the branched chain amino acids leucine , isoleucine , and valine 2 . 1 cite web url http www.rcsb.org pdb explore explore.do?structureId 3DTF title RCSB Protein Data Bank Structure Summary for 3DTF Structural analysis of mycobacterial branched chain aminotransferase implications for inhibitor design format work accessdate 2 cite web url http www.ncbi.nlm.nih.gov sites entrez?Db pubmed&Cmd Retrieve&list uids 11642362&dopt abstractplus title Structure and function of branched chain aminotran... Prog Nucleic Acid Res Mol Biol. 2001 PubMed result format work accessdate External links MeshName branched chain amino acid transaminase cite web url http www.rcsb.org pdb explore explore.do?structureId 3DTF title RCSB Protein Data Bank Structure Summary for 3DTF Structural analysis of mycobacte ... more details
enzyme Name 2 methylacyl CoA dehydrogenase EC number 1.3.99.12 CAS number 85130 32 1 IUBMB EC number 1 3 99 12 GO code 0003853 image width caption In enzymology , a 2 methylacyl CoA dehydrogenase EC number 1.3.99.12 is an enzyme that catalysis catalyzes the chemical reaction 2 methylbutanoyl CoA acceptor math rightleftharpoons math 2 methylbut 2 enoyl CoA reduced acceptor Thus, the two substrate biochemistry substrates of this enzyme are 2 methylbutanoyl CoA and Electron acceptor acceptor , whereas its two product chemistry products are 2 methylbut 2 enoyl CoA and reduced acceptor . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH CH group of donor with other acceptors. The systematic name of this enzyme class is 2 methylbutanoyl CoA acceptor oxidoreductase . Other names in common use include branched chain acyl CoA dehydrogenase , 2 methyl branched chain acyl CoA dehydrogenase , and 2 methylbutanoyl CoA acceptor oxidoreductase . This enzyme participates in valine, leucine and isoleucine degradation . References reflist 1 cite journal author Ikeda Y, Dabrowski C, Tanaka K date 1983 title Separation and properties of five distinct acyl CoA dehydrogenases from rat liver mitochondria. Identification of a new 2 methyl branched chain acyl CoA dehydrogenase journal J. Biol. Chem. volume 258 pages 1066&ndash 76 pmid 6401712 issue 2 1.3 enzyme stub Category EC 1.3.99 Category Enzymes of unknown structure it 2 metilacil CoA deidrogenasi ja 2 CoA ... more details
enzyme Name 2 oxoisovalerate dehydrogenase acylating EC number 1.2.1.25 CAS number 37211 61 3 IUBMB EC number 1 2 1 25 GO code 0047101 image width caption In enzymology , a 2 oxoisovalerate dehydrogenase acylating EC number 1.2.1.25 is an enzyme that catalysis catalyzes the chemical reaction 3 methyl 2 oxobutanoate CoA NAD sup sup math rightleftharpoons math 2 methylpropanoyl CoA CO sub 2 sub NADH The 3 substrate biochemistry substrates of this enzyme are 3 methyl 2 oxobutanoate , coenzyme A CoA , and nicotinamide adenine dinucleotide NAD sup sup , whereas its 3 product chemistry products are 2 methylpropanoyl CoA , carbon dioxide CO sub 2 sub , and nicotinamide adenine dinucleotide NADH . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is 3 methyl 2 oxobutanoate NAD 2 oxidoreductase CoA methyl propanoylating . Other names in common use include 2 oxoisovalerate dehydrogenase , and alpha ketoisovalerate dehydrogenase . This enzyme participates in valine, leucine and isoleucine degradation . References reflist 1 cite journal author Namba Y, Yoshizawa K, Ejima A, Hayashi T, Kaneda T date 1969 title Coenzyme A and nicotinamide adenine dinucleotide dependent branched chain alpha keto acid dehydrogenase. I. Purification and properties of the enzyme from Bacillus subtilis journal J. Biol. Chem. volume 244 pages 4437&ndash 47 pmid 4308861 issue 16 1.2 enzyme stub Category EC 1.2.1 Category NADH dependent enzymes Category Enzymes of unknown structure it 2 ossoisovalerato deidrogenasi acilante ja 2 ... more details
enzyme Name leucine 2,3 aminomutase EC number 5.4.3.7 CAS number 59125 53 0 IUBMB EC number 5 4 3 7 GO code 0050047 image width caption In enzymology , a leucine 2,3 aminomutase EC number 5.4.3.7 is an enzyme that catalysis catalyzes the chemical reaction 2S alpha leucine math rightleftharpoons math 3R beta leucine Hence, this enzyme has one substrate biochemistry substrate , 2S alpha leucine , and one product chemistry product , 3R beta leucine . This enzyme belongs to the family of isomerase s, specifically those intramolecular transferase s transferring amino groups. The systematic name of this enzyme class is 2S alpha leucine 2,3 aminomutase . This enzyme participates in valine, leucine and isoleucine degradation . It employs one cofactor biochemistry cofactor , cobamide . References reflist 1 cite journal author Freer I, Pedrocchi Fantoni G, Picken DJ and Overton KH date 1981 title Stereochemistry of the leucine 2,3 aminomutase from tissue cultures of Andrographis paniculata journal J. Chem. Soc. Chem. volume Commun. pages 80&ndash 82 cite journal author Poston JM date 1976 title Leucine 2,3 aminomutase, an enzyme of leucine catabolism journal J. Biol. Chem. volume 251 pages 1859&ndash 63 pmid 1270414 issue 7 cite journal author Poston JM date 1976 title Coenzyme B12 dependent enzymes in potatoes leucine 2,3 aminomutase and methylmalonyl CoA mutase journal Phytochemistry journal Phytochemistry volume 17 pages 401&ndash 402 doi 10.1016 S0031 9422 00 89324 3 issue 3 Category EC 5.4.3 Category Cobamide enzymes Category Enzymes of unknown structure isomerase stub ... more details
enzyme Name acetolactate decarboxylase EC number 4.1.1.5 CAS number 9025 02 9 IUBMB EC number 4 1 1 5 GO code 0047605 image width caption In enzymology , an acetolactate decarboxylase EC number 4.1.1.5 is an enzyme that catalysis catalyzes the chemical reaction S 2 hydroxy 2 methyl 3 oxobutanoate math rightleftharpoons math R 2 acetoin CO sub 2 sub Hence, this enzyme has one substrate biochemistry substrate , Acetolactate S 2 hydroxy 2 methyl 3 oxobutanoate , and two product chemistry products , R 2 acetoin and carbon dioxide CO sub 2 sub . This enzyme belongs to the family of lyase s, specifically the carboxy lyases, which cleave carbon carbon bonds. The systematic name of this enzyme class is S 2 hydroxy 2 methyl 3 oxobutanoate carboxy lyase R 2 acetoin forming . Other names in common use include alpha acetolactate decarboxylase , and S 2 hydroxy 2 methyl 3 oxobutanoate carboxy lyase . This enzyme participates in butanoate metabolism and c5 branched dibasic acid metabolism . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1XV2 . References reflist 1 cite journal author Hill RK, Sawada S and Arfin SM date 1979 title Stereochemistry of valine and isoleucine biosynthesis. IV Synthesis, configuration, and enzymatic specificity of alpha acetolactate and alpha aceto alpha hydroxybutyrate journal Bioorg. Chem. volume 8 pages 175&ndash 189 doi 10.1016 0045 2068 79 90003 8 issue 2 cite journal author Stormer FC date 1967 title Isolation of crystalline pH 6 acetolactate forming enzyme from Aerobacter aerogenes journal J. Biol. Chem. volume 242 pages 1756&ndash 9 pmid 6024768 issue 8 4.1 enzyme stub Category EC 4.1.1 Category Enzymes of known structure ... more details
enzyme Name hydroxymethylglutaryl CoA synthase EC number 2.3.3.10 CAS number 9027 44 5 IUBMB EC number 2 3 3 10 GO code 0004421 image width caption In enzymology , a hydroxymethylglutaryl CoA synthase EC number 2.3.3.10 is an enzyme that catalysis catalyzes the chemical reaction acetyl CoA H sub 2 sub O acetoacetyl CoA math rightleftharpoons math S 3 hydroxy 3 methylglutaryl CoA CoA The 3 substrate biochemistry substrates of this enzyme are acetyl CoA , water H sub 2 sub O , and acetoacetyl CoA , whereas its two product chemistry products are S 3 hydroxy 3 methylglutaryl CoA and coenzyme A CoA . This enzyme belongs to the family of transferase s, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl CoA acetoacetyl CoA C acetyltransferase thioester hydrolysing, carboxymethyl forming . Other names in common use include S 3 hydroxy 3 methylglutaryl CoA acetoacetyl CoA lyase , CoA acetylating , 3 hydroxy 3 methylglutaryl CoA synthetase , 3 hydroxy 3 methylglutaryl coenzyme A synthase , 3 hydroxy 3 methylglutaryl coenzyme A synthetase , 3 hydroxy 3 methylglutaryl CoA synthase , 3 hydroxy 3 methylglutaryl coenzyme A synthase , beta hydroxy beta methylglutaryl CoA synthase , HMG CoA synthase , acetoacetyl coenzyme A transacetase , hydroxymethylglutaryl coenzyme A synthase , and hydroxymethylglutaryl coenzyme A condensing enzyme . This enzyme participates in 3 metabolism metabolic pathways synthesis and degradation of ketone bodies , valine, leucine and isoleucine degradation , and butanoate metabolism . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1XPK , PDB link 1XPL , PDB link 1XPM , and PDB link 2P8U . References reflist 1 cite journal author RUDNEY H date 1957 title The biosynthesis of beta hydroxy beta methylglutaric acid journal J. Biol. Chem. volume 227 pages 3 ... more details
enzyme Name beta alanine pyruvate transaminase EC number 2.6.1.18 CAS number 9030 47 1 IUBMB EC number 2 6 1 18 GO code 0016223 image width caption In enzymology , a beta alanine pyruvate transaminase EC number 2.6.1.18 is an enzyme that catalysis catalyzes the chemical reaction L alanine 3 oxopropanoate math rightleftharpoons math pyruvate beta alanine Thus, the two substrate biochemistry substrates of this enzyme are L alanine and 3 oxopropanoate , whereas its two product chemistry products are pyruvate and beta 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 alanine 3 oxopropanoate aminotransferase . Other names in common use include beta alanine pyruvate aminotransferase , and beta alanine alpha alanine transaminase . This enzyme participates in 4 metabolism metabolic pathways alanine and aspartate metabolism , valine, leucine and isoleucine degradation , beta alanine metabolism , and propanoate metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S date 1961 title Enzymatic studies on the metabolism of beta alanine journal J. Biol. Chem. volume 236 pages 781&ndash 90 pmid 13712439 cite journal author Stinson RA, Spencer MS date 1969 title Beta alanine aminotransferase s from a plant source journal Biochem. Biophys. Res. Commun. volume 34 pages 120&ndash 7 pmid 5762452 doi 10.1016 0006 291X 69 90537 3 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name S 3 amino 2 methylpropionate transaminase EC number 2.6.1.22 CAS number 9031 95 2 IUBMB EC number 2 6 1 22 GO code 0047298 image width caption In enzymology , a S 3 amino 2 methylpropionate transaminase EC number 2.6.1.22 is an enzyme that catalysis catalyzes the chemical reaction S 3 amino 2 methylpropanoate 2 oxoglutarate math rightleftharpoons math 2 methyl 3 oxopropanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are S 3 amino 2 methylpropanoate and 2 oxoglutarate , whereas its two product chemistry products are 2 methyl 3 oxopropanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is S 3 amino 2 methylpropanoate 2 oxoglutarate aminotransferase . Other names in common use include L 3 aminoisobutyrate transaminase , beta aminobutyric transaminase , L 3 aminoisobutyric aminotransferase , and beta aminoisobutyrate alpha ketoglutarate transaminase . This enzyme participates in valine, leucine and isoleucine degradation . References reflist 1 cite journal author Kakimoto Y, Kanazawa A, Taniguchi K, Sano I date 1968 title Beta aminoisobutyrate alpha ketoglutarate transaminase in relation to beta aminoisobutyric aciduria journal Biochim. Biophys. Acta. volume 156 pages 374&ndash 80 pmid 5641913 issue 2 cite journal author Tamaki N, Sakata SF, Matsuda K date 2000 title Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver journal Methods Enzymol. volume 324 pages 376&ndash 89 pmid 10989446 doi 10.1016 S0076 6879 00 24247 X series Methods in Enzymology isbn 9780121822255 Category EC 2.6.1 Category Enzymes of unknown structure transferase stub ... more details
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