In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively:[2]
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. This enzyme participates in the metabolism of glycine, serine, threonine and also methionine.
BHMT is expressed most predominantly in the liver and kidney.[7]
Clinical significanceedit
Mutations in the BHMT gene are known to exist in humans. Anomalies may influence the metabolism of homocysteine , which is implicated in disorders ranging from vascular disease, autism, and schizophrenia to neural tube birth defects such as spina bifida.
^PDB: 1UMY; González B, Pajares MA, Martínez-Ripoll M, Blundell TL, Sanz-Aparicio J (May 2004). "Crystal structure of rat liver betaine homocysteine s-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding". J. Mol. Biol. 338 (4): 771–82. CiteSeerX10.1.1.320.5080. doi:10.1016/j.jmb.2004.03.005. PMID 15099744.
^Pajares MA, Pérez-Sala D (December 2006). "Betaine homocysteine S-methyltransferase: just a regulator of homocysteine metabolism?". Cell. Mol. Life Sci. 63 (23): 2792–803. doi:10.1007/s00018-006-6249-6. hdl:10261/13799. PMID 17086380. S2CID 6076708.
^Garrow TA (September 1996). "Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase". J. Biol. Chem. 271 (37): 22831–8. doi:10.1074/jbc.271.37.22831. PMID 8798461.
^Sunden SL, Renduchintala MS, Park EI, Miklasz SD, Garrow TA (September 1997). "Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene". Arch. Biochem. Biophys. 345 (1): 171–4. doi:10.1006/abbi.1997.0246. PMID 9281325.
^Chadwick LH, McCandless SE, Silverman GL, Schwartz S, Westaway D, Nadeau JH (November 2000). "Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes". Genomics. 70 (1): 66–73. doi:10.1006/geno.2000.6319. PMID 11087663.
^Szegedi SS, Castro CC, Koutmos M, Garrow TA (April 2008). "Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase". J. Biol. Chem. 283 (14): 8939–45. doi:10.1074/jbc.M710449200. PMC2276374. PMID 18230605.
^Sunden SL, Renduchintala MS, Park EI, Miklasz SD, Garrow TA (September 1997). "Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene". Arch. Biochem. Biophys. 345 (1): 171–4. doi:10.1006/abbi.1997.0246. PMID 9281325.
Further readingedit
Klee WA, Richards HH, Cantoni GL (1961). "The synthesis of methionine by enzymic transmethylation. VII Existence of two separate homocysteine methylpherases on mammalian liver". Biochim. Biophys. Acta. 54: 157–64. doi:10.1016/0006-3002(61)90948-9. PMID 14456704.
External linksedit
Betaine+Homocysteine+Methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
betaine, homocysteine, methyltransferase, field, enzymology, betaine, homocysteine, methyltransferase, also, known, betaine, homocysteine, methyltransferase, bhmt, zinc, metallo, enzyme, that, catalyzes, transfer, methyl, group, from, trimethylglycine, hydroge. In the field of enzymology a betaine homocysteine S methyltransferase also known as betaine homocysteine methyltransferase BHMT is a zinc metallo enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively 2 Trimethylglycine methyl donor homocysteine hydrogen donor dimethylglycine hydrogen receiver methionine methyl receiver betaine homocysteine S methyltransferaseCrystal structure of rat liver betaine homocysteine s methyltransferase 1 IdentifiersEC no 2 1 1 5CAS no 9029 78 1DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins Diagram of the action of BHMTThis enzyme belongs to the family of transferases specifically those transferring one carbon group methyltransferases This enzyme participates in the metabolism of glycine serine threonine and also methionine Contents 1 Isozymes 2 Tissue distribution 3 Clinical significance 4 See also 5 References 6 Further reading 7 External linksIsozymes editIn humans there are two isozymes BHMT 3 4 and BHMT2 5 6 each encoded by a separate gene betaine homocysteine methyltransferase nbsp Betaine homocysteine S methyltransferase 1 homotetramer HumanIdentifiersSymbolBHMTNCBI gene635HGNC1047OMIM602888RefSeqNM 001713UniProtQ93088Other dataEC number2 1 1 5LocusChr 5 q13 1 q15Search forStructuresSwiss modelDomainsInterPro betaine homocysteine methyltransferase 2IdentifiersSymbolBHMT2NCBI gene23743HGNC1048OMIM605932RefSeqNM 017614UniProtQ9H2M3Other dataEC number2 1 1 5LocusChr 5 q13Search forStructuresSwiss modelDomainsInterProTissue distribution editBHMT is expressed most predominantly in the liver and kidney 7 Clinical significance editMutations in the BHMT gene are known to exist in humans Anomalies may influence the metabolism of homocysteine which is implicated in disorders ranging from vascular disease autism and schizophrenia to neural tube birth defects such as spina bifida See also editBetaineReferences edit PDB 1UMY Gonzalez B Pajares MA Martinez Ripoll M Blundell TL Sanz Aparicio J May 2004 Crystal structure of rat liver betaine homocysteine s methyltransferase reveals new oligomerization features and conformational changes upon substrate binding J Mol Biol 338 4 771 82 CiteSeerX 10 1 1 320 5080 doi 10 1016 j jmb 2004 03 005 PMID 15099744 Pajares MA Perez Sala D December 2006 Betaine homocysteine S methyltransferase just a regulator of homocysteine metabolism Cell Mol Life Sci 63 23 2792 803 doi 10 1007 s00018 006 6249 6 hdl 10261 13799 PMID 17086380 S2CID 6076708 Garrow TA September 1996 Purification kinetic properties and cDNA cloning of mammalian betaine homocysteine methyltransferase J Biol Chem 271 37 22831 8 doi 10 1074 jbc 271 37 22831 PMID 8798461 Sunden SL Renduchintala MS Park EI Miklasz SD Garrow TA September 1997 Betaine homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene Arch Biochem Biophys 345 1 171 4 doi 10 1006 abbi 1997 0246 PMID 9281325 Chadwick LH McCandless SE Silverman GL Schwartz S Westaway D Nadeau JH November 2000 Betaine homocysteine methyltransferase 2 cDNA cloning gene sequence physical mapping and expression of the human and mouse genes Genomics 70 1 66 73 doi 10 1006 geno 2000 6319 PMID 11087663 Szegedi SS Castro CC Koutmos M Garrow TA April 2008 Betaine homocysteine S methyltransferase 2 is an S methylmethionine homocysteine methyltransferase J Biol Chem 283 14 8939 45 doi 10 1074 jbc M710449200 PMC 2276374 PMID 18230605 Sunden SL Renduchintala MS Park EI Miklasz SD Garrow TA September 1997 Betaine homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene Arch Biochem Biophys 345 1 171 4 doi 10 1006 abbi 1997 0246 PMID 9281325 Further reading editKlee WA Richards HH Cantoni GL 1961 The synthesis of methionine by enzymic transmethylation VII Existence of two separate homocysteine methylpherases on mammalian liver Biochim Biophys Acta 54 157 64 doi 10 1016 0006 3002 61 90948 9 PMID 14456704 External links editBetaine Homocysteine Methyltransferase at the U S National Library of Medicine Medical Subject Headings MeSH EC 2 1 1 5 Portal nbsp Biology This EC 2 1 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Betaine homocysteine S methyltransferase amp oldid 1191246960, wikipedia, wiki, book, books, library,
