Methylenetetrahydrofolate reductase: A common human polymorphism and its biochemical implications
dc.contributor.author | Matthews, Rowena Green | en_US |
dc.date.accessioned | 2006-04-19T14:21:36Z | |
dc.date.available | 2006-04-19T14:21:36Z | |
dc.date.issued | 2002 | en_US |
dc.identifier.citation | Matthews, Rowena G. (2002)."Methylenetetrahydrofolate reductase: A common human polymorphism and its biochemical implications." The Chemical Record 2(1): 4-12. <http://hdl.handle.net/2027.42/35288> | en_US |
dc.identifier.issn | 1527-8999 | en_US |
dc.identifier.issn | 1528-0691 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/35288 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11933257&dopt=citation | en_US |
dc.description.abstract | Methlenetetrahydrofolate (CH 2 -H 4 folate) is required for the conversion of homocysteine to methionine and of dUMP to dTMP in support of DNA synthesis, and also serves as a major source of one carbon unit for purine biosynthesis. This review presents biochemical studies of a human polymorphism in methylenetetrahydrofolate reductase, which catalyzes the reaction shown below. The mutation decreases the flux of CH 2 -H 4 folate into CH 3 -H 4 folate, and is associated with both beneficial and deleterious effects that can be traced to the molecular effect of the substitution of alanine 222 by valine. © 2002 The Japan Chemical Journal Forum and John Wiley & Sons, Inc. Chem Rec 2: 4–12, 2002 | en_US |
dc.format.extent | 380196 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | John Wiley & Sons, Inc. | en_US |
dc.subject.other | Chemistry | en_US |
dc.title | Methylenetetrahydrofolate reductase: A common human polymorphism and its biochemical implications | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division, The University of Michigan, 930 N. University Avenue, Ann Arbor, Michigan 48109-1055 ; Department of Biological Chemistry, The University of Michigan, 930 N. University Avenue, Ann Arbor, Michigan 48109-1055 ; Biophysics Research Division and Department of Biological Chemistry, The University of Michigan, 930 N. University Avenue, Ann Arbor, Michigan 48109-1055 | en_US |
dc.identifier.pmid | 11933257 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/35288/1/10006_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/tcr.10006 | en_US |
dc.identifier.source | The Chemical Record | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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