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Structure paper

TitleEvidence in Support of Lysine 77 and Histidine 96 as Acid-Base Catalytic Residues in Saccharopine Dehydrogenase from Saccharomyces cerevisiae.
Journal, issue, pagesBiochemistry, Vol. 51, Page 857-866, Year 2012
Publish dateNov 2, 2011 (structure data deposition date)
AuthorsKumar, V.P. / Thomas, L.M. / Bobyk, K.D. / Andi, B. / Cook, P.F. / West, A.H.
External linksBiochemistry / PubMed:22243403
MethodsX-ray diffraction
Resolution2.01 - 2.3 Å
Structure data

PDB-3ugk:
Crystal Structure of C205S mutant and Saccharopine Dehydrogenase from Saccharomyces cerevisiae.
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-3uh1:
Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae with bound saccharopine and NADH
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

PDB-3uha:
Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cervisiae complexed with NAD.
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-SHR:
N-(5-AMINO-5-CARBOXYPENTYL)GLUTAMIC ACID

ChemComp-GOL:
GLYCEROL

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

ChemComp-CL:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsOXIDOREDUCTASE / lysine biosynthesis / proton shuttle / enzyme mechanisms / Saccharopine and NAD binding / enzyme mechanism / NAD binding

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