Abstract:
:The crystal structure of a ternary complex of meso-2,3-butanediol dehydrogenase with NAD+ and a competitive inhibitor, mercaptoethanol, has been determined at 1.7 A resolution by means of molecular replacement and refined to a final R-factor of 0.194. The overall structure is similar to those of the other short chain dehydrogenase/reductase enzymes. The NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues around the active site, Gln140 and Gly183, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Otagiri M,Kurisu G,Ui S,Takusagawa Y,Ohkuma M,Kudo T,Kusunoki Mdoi
10.1093/oxfordjournals.jbchem.a002845keywords:
subject
Has Abstractpub_date
2001-02-01 00:00:00pages
205-8issue
2eissn
0021-924Xissn
1756-2651journal_volume
129pub_type
杂志文章abstract::During a large-scale in vitro translation analysis of a human full-length cDNA bank, we found many clones producing in vitro translation products showing ladder bands on a fluorogram with the equidistance of about 9 kDa at the position larger than the molecular mass expected from the open reading frame. We have analyz...
journal_title:Journal of biochemistry
pub_type: 杂志文章
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更新日期:1999-07-01 00:00:00
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journal_title:Journal of biochemistry
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pub_type: 杂志文章
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journal_title:Journal of biochemistry
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更新日期:2011-09-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a134719
更新日期:1984-04-01 00:00:00
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a132589
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:
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