New developments in our understanding of the β-hydroxyacid dehydrogenases

Chemico-Biological Interactions

Volumn 130, Issue 132, 2001, Pages 785-791

  Njau, R K ^a   Herndon, C A ^a   Hawes, J W ^a  

^a INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Dehydrogenase; Hydroxyacid; Hydroxybutyrate; Tartronate semialdehyde

Indexed keywords

D 2 HYDROXY ACID DEHYDROGENASE; GLYCERIC ACID; ISOBUTYRIC ACID DERIVATIVE; LYSINE; OXIDOREDUCTASE; TARTRONIC ACID DERIVATIVE; THREONINE; TRINITROBENZENESULFONIC ACID; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; CATALYSIS; CONFERENCE PAPER; ENERGY CONSERVATION; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INACTIVATION; HAEMOPHILUS INFLUENZAE; MOLECULAR CLONING; NONHUMAN; OXIDATION; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; CARBOHYDRATE DEHYDROGENASES; CONSERVED SEQUENCE; ESCHERICHIA COLI; HAEMOPHILUS INFLUENZAE; LYSINE; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS);

EID: 0035969876     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(00)00234-9     Document Type: Article

References (5)

1. Structural and mechanistic similarities of 6-phosphogluconate and β-hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the β-hydroxy acid dehydrogenases
2. Structural and mechanistic aspects of a new family of dehydrogenases: The β-hydroxyacid dehydrogenases
3. Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: Implications for NADP specificity and the enzyme mechanism
4. Lysine 183 is the general base in the 6-phosphogluconate dehydrogenase-catalyzed reaction
5. Use of trinitrobenzensulfonate for affinity labeling of lysine residues at phosphate binding sites of some enzymes