| Comment | One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (PF00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (PMID:11577733). |
| References | RN [1]
RM 8444801
RT Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes.
RA Blomqvist K, Nikkola M, Lehtovaara P, Suihko ML, Airaksinen U, Straby KB, Knowles JK, Penttila ME.
DR PFAM; PF00106; adh_short
RN [2]
RM 9332371
RT Molecular cloning and characterization of a cDNA encoding a bovine butanediol dehydrogenase.
RA Smania AM, Argarana CE.
RL Gene. 1997 Sep 15;197(1-2):231-8.
RN [3]
RM 11173520
RT Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms.
RA Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M.
RL J Biochem (Tokyo). 2001 Feb;129(2):205-8.
RN [4]
RM 11577733
RT Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli.
RA Takusagawa Y, Otagiri M, Ui S, Ohtsuki T, Mimura A, Ohkuma M, Kudo T.
RL Biosci Biotechnol Biochem. 2001 Aug;65(8):1876-8. |
