1.1.1.345: D-2-hydroxyacid dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about D-2-hydroxyacid dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.1.1.345
Reaction
Synonyms
D-2-HADH, D-2-hydroxyacid dehydrogenase, D-2-hydroxyisocaproate dehydrogenase, D-HicDH, D-isomer specific 2-hydroxyacid dehydrogenase, D-isomer specific NAD+-dependent 2-hydroxyacid dehydrogenase, D-isomer-specific 2-hydroxyacid dehydrogenase, D-lactate dehydrogenase, D-lactate:NAD+ oxidoreductase, D-malate dehydrogenases, D-mandelate dehydrogenase, D-ManDH1, D-ManDH2, D-MDH, D2-HDH, HdhD, Ldb1010, ldh1837, LEUM_1837, ManDH2, NAD-dependent D-2-hydroxyacid dehydrogenase, PanE, R-HicDH
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Reference on EC 1.1.1.345 - D-2-hydroxyacid dehydrogenase (NAD+)
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, T.; Yang, W.; Pereira, A.C.; Craigen, W.J.; Shih, V.E.
Cloning and characterization of a putative human D-2-hydroxyacid dehydrogenase in chromosome 9q
Biochem. Biophys. Res. Commun.
268
298-301
2000
Homo sapiens
Bonete, M.J.; Ferrer, J.; Pire, C.; Penades, M.; Ruiz, J.L.
2-Hydroxyacid dehydrogenase from Haloferax mediteranii, a D-isomer-specific member of the 2-dehydrogenase family
Biochimie
82
1143-1150
2000
Haloferax mediterranei, Haloferax mediterranei R4, ATCC 33500
Wada, Y.; Iwai, S.; Tamura, Y.; Ando, T.; Shinoda, T.; Arai, K.; Taguchi, H.
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases
Biosci. Biotechnol. Biochem.
72
1087-1094
2008
Enterococcus faecalis
Domenech, J.; Baker, P.; Sedelnikova, S.; Rodgers, H.; Rice, D.; Ferrer, J.
Crystallization and preliminary X-ray analysis of D-2-hydroxyacid dehydrogenase from Haloferax mediterranei
Acta Crystallogr. Sect. F
65
415-418
2009
Haloferax mediterranei, Haloferax mediterranei ATCC 335500
Chambellon, E.; Rijnen, L.; Lorquet, F.; Gitton, C.; Van Hylckama Vlieg, J.; Wouters, J.; Yvon, M.
The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis
J. Bacteriol.
191
873-881
2009
Lactococcus lactis, Lactococcus cremoris, Lactococcus lactis IL1403, Lactococcus cremoris TIL46
Taguchi, H.; Ohta, T.
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family: Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum
J. Biol. Chem.
266
12588-12594
1991
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC 8041
Niefind, K.; Hecht, H.J.; Schomburg, D.
Crystallization and preliminary characterization of crystals of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei
J. Mol. Biol.
240
400-402
1994
Lacticaseibacillus paracasei (P17584)
Dengler, U.; Niefind, K.; Kiess, M.; Schomburg, D.
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution
J. Mol. Biol.
267
640-660
1997
Lacticaseibacillus paracasei (P17584)
Tamura, Y.; Ohkubo, A.; Iwai, S.; Wada, Y.; Shinoda, T.; Arai, K.; Mineki, S.; Iida, M.; Taguchi, H.
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
Appl. Environ. Microbiol.
68
947-951
2002
Enterococcus faecalis
Miyanaga, A.; Fujisawa, S.; Furukawa, N.; Arai, K.; Nakajima, M.; Taguchi, H.
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase
Biochem. Biophys. Res. Commun.
439
109-114
2013
Enterococcus faecium (E3USM3)
Hummel, W.; Schütte, H.; Kula, M.-R.
D-2-Hydroxyisocaproate dehydrogenase from Lactobacillus casei
Appl. Microbiol. Biotechnol.
21
7-15
1985
Lacticaseibacillus paracasei (P17584)
-
Kallwass, H.K.W.
Potential of R-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei for stereospecific reductions
Enzyme Microb. Technol.
14
28-35
1992
Lacticaseibacillus casei
-
Bernard, N.; Johnsen, K.; Ferain, T.; Garmyn, D.; Hols, P.; Holbrook, J.J.; Delcour, J.
NAD(+)-dependent D-2-hydroxyisocaproate dehydrogenase of Lactobacillus delbrueckii subsp. bulgaricus. Gene cloning and enzyme characterization
Eur. J. Biochem.
224
439-446
1994
Lactobacillus delbrueckii (Q48534), Lactobacillus delbrueckii
Holton, S.; Anandhakrishnan, M.; Geerlof, A.; Wilmanns, M.
Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus
J. Struct. Biol.
181
179-184
2013
Lactobacillus delbrueckii subsp. bulgaricus (Q1GAA2), Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 (Q1GAA2)
Kim, K.H.; Jia, X.; Jia, B.; Jeon, C.O.
Identification and characterization of the L-malate dehydrogenases and L-lactate biosynthetic pathway in Leuconostoc mesenteroides ATCC 8293
J. Agric. Food Chem.
66
8086-8093
2018
Leuconostoc mesenteroides subsp. mesenteroides (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides BCRC 11652 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NCDO 523 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NRRL B-1118 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NCTC 12954 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides JCM 6124 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NBRC 100496 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides DSM 20343 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides 37Y (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NCIMB 8023 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides CCM 1803 (Q03V58)
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