Sequence of LDHD_LACDA
EC Number:1.1.1.28
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
D-lactate dehydrogenase
P26297
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14)
333
37049
Reaction
(R)-lactate + NAD+ = pyruvate + NADH + H+
Other sequences found for EC No. 1.1.1.28
General information:
Sequence
0 MTKIFAYAIR EDEKPFLKEW EDAHKDVEVE YTDKLLTPET VALAKGADGV VVYQQLDYTA
60 ETLQALADNG ITKMSLRNVG VDNIDMAKAK ELGFQITNVP VYSPNAIAEH AAIQAARILR
120 QDKAMDEKVA RHDLRWAPTI GREVRDQVVG VIGTGHIGQV FMQIMEGFGA KVIAYDIFRN
180 PELEKKGYYV DSLDDLYKQA DVISLHVPDV PANVHMINDE SIAKMKQDVV IVNVSRGPLV
240 DTDAVIRGLD SGKIFGYAMD VYEGEVGIFN EDWEGKEFPD ARLADLIARP NVLVTPHTAF
300 YTTHAVRNMV VKAFDNNLEL VEGKEAETPV KVG
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1207136
Bernard N.,Ferain T.,Garmyn D.,Hols P.,Delcour J.
Cloning of the D-lactate dehydrogenase gene from Lactobacillus delbrueckii subsp. bulgaricus by complementation in Escherichia coli.
FEBS Lett.
290
61-64
1991
1207137
Kochhar S.,Hunziker P.,Leong-Morgenthaler P.M.,Hottinger H.
Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site.
J. Biol. Chem.
267
8499-8513
1992
1207138
Kochhar S.,Chuard N.,Hottinger H.
Cloning and overexpression of the Lactobacillus bulgaricus NAD(+)-dependent D-lactate dehydrogenase gene in Escherichia coli: purification and characterization of the recombinant enzyme.
Biochem. Biophys. Res. Commun.
185
705-712
1992
1207139
van de Guchte M.,Penaud S.,Grimaldi C.,Barbe V.,Bryson K.,Nicolas P.,Robert C.,Oztas S.,Mangenot S.,Couloux A.,Loux V.,Dervyn R.,Bossy R.,Bolotin A.,Batto J.-M.,Walunas T.,Gibrat J.-F.,Bessieres P.,Weissenbach J.,Ehrlich S.D.,Maguin E.
The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution.
Proc. Natl. Acad. Sci. U.S.A.
103
9274-9279
2006
1207140
Kochhar S.,Hunziker P.,Leong-Morgenthaler P.M.,Hottinger H.
Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.
Biochem. Biophys. Res. Commun.
184
60-66
1992
1207141
Bernard N.,Johnsen K.,Gelpi J.L.,Alvarez J.A.,Ferain T.,Garmyn D.,Hols P.,Cortes A.,Clarke A.R.,Holbrook J.J.,Delcour J.
D-2-hydroxy-4-methylvalerate dehydrogenase from Lactobacillus delbrueckii subsp. bulgaricus. II. Mutagenic analysis of catalytically important residues.
Eur. J. Biochem.
244
213-219
1997
1207142
Vinals C.,Depiereux E.,Feytmans E.
Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase.
Biochem. Biophys. Res. Commun.
192
182-188
1993
1207143
Razeto A.,Kochhar S.,Hottinger H.,Dauter M.,Wilson K.S.,Lamzin V.S.
Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.
J. Mol. Biol.
318
109-119
2002
