Back to Search
Start Over
Substrate recognition of isocitrate dehydrogenase and 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8.
- Source :
-
Journal of biochemistry [J Biochem] 1997 Jan; Vol. 121 (1), pp. 77-81. - Publication Year :
- 1997
-
Abstract
- The substrate-binding sites of NADP-dependent isocitrate dehydrogenase and NAD-dependent 3-isopropylmalate dehydrogenase from Thermus thermophilus were analyzed by site-directed mutagenesis. Ser97 and Asn99 of isocitrate dehydrogenase were identified to be involved in the isocitrate recognition. In 3-isopropylmalate dehydrogenase, the corresponding residues, Leu90 and Leu91, appear to recognize the substrate by forming a hydrophobic pocket. Double mutation of Asp78 and Glu87 revealed that negative charge of these residues plays a crucial role in discriminating isopropylmalate from isocitrate.
- Subjects :
- 3-Isopropylmalate Dehydrogenase
Alcohol Oxidoreductases genetics
Amino Acid Sequence
Asparagine genetics
Asparagine metabolism
Aspartic Acid genetics
Aspartic Acid metabolism
Binding Sites
Glutamic Acid genetics
Glutamic Acid metabolism
Isocitrate Dehydrogenase genetics
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Serine genetics
Serine metabolism
Substrate Specificity
Alcohol Oxidoreductases metabolism
Isocitrate Dehydrogenase metabolism
Thermus thermophilus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-924X
- Volume :
- 121
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 9058195
- Full Text :
- https://doi.org/10.1093/oxfordjournals.jbchem.a021573