Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax

Journal of Molecular Biology

Volumn 341, Issue 3, 2004, Pages 815-828

  Lorentzen, Esben ^a   Hensel, Reinhard ^b   Knura, Thomas ^b   Ahmed, Hatim ^b   Pohl, Ehmke ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF DUISBURG ESSEN   (Germany)

Author keywords

aldehyde dehydrogenase; ALDH, aldehyde dehydrogenases; allosteric regulation; crystal structure; EMP, Embden Meyerhof Parnas; GAPN, glyceraldehyde 3 phosphate dehydrogenase; glyceraldehyde 3 phosphate dehydrogenase

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; FRUCTOSE; GLUCOSE 1 PHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NUCLEOTIDE; PYRIDINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ALLOSTERISM; ARTICLE; BACTERIAL STRAIN; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; THERMOPROTEUS TENAX;

THERMOPROTEUS; THERMOPROTEUS TENAX;

EID: 4344591748     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.032     Document Type: Article

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