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Structure paper

TitleDomain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.
Journal, issue, pagesJ. Mol. Biol., Vol. 318, Page 109-119, Year 2002
Publish dateAug 14, 2001 (structure data deposition date)
AuthorsRazeto, A. / Kochhar, S. / Hottinger, H. / Dauter, M. / Wilson, K.S. / Lamzin, V.S.
External linksJ. Mol. Biol. / PubMed:12054772
MethodsX-ray diffraction
Resolution1.9 - 2.2 Å
Structure data

PDB-1j49:
INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1j4a:
INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • lactobacillus delbrueckii subsp. bulgaricus (bacteria)
KeywordsOXIDOREDUCTASE / NAD-DEPENDENT DEHYDROGENASE / LAST STEP OF GLYCOLYSIS UNDER ANAEROBIC CONDITIONS / REVERSIBLE INTERCONVERSION OF PYRUVATE INTO D-LACTATE

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