Octopine dehydrogenase from Pecten maximus: steady-state mechanism
- 27 March 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (7) , 1348-1353
- https://doi.org/10.1021/bi00302a002
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 8 references indexed in Scilit:
- Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenaseBiochemistry, 1981
- Kinetic mechanism of glutamate dehydrogenaseBiochemistry, 1980
- Purification and Characterization of the Crown Gall-specific Enzyme, Octopine SynthasePlant Physiology, 1980
- Glutamate synthase: the kinetic mechanism of the enzyme from Escherichia coli WBiochemistry, 1978
- Investigation on the Kinetic Mechanism of Octopine Dehydrogenase. A Regulatory BehaviorEuropean Journal of Biochemistry, 1978
- Properties of d(+)-lysopine dehydrogenase from crown gall tumour tissueBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Stereochemistry of octopine and of its isomers and their enzymatic propertiesBioorganic Chemistry, 1977
- USE OF COPPER (II) ION IN MASKING α-AMINO GROUPS OF AMINO ACIDSJournal of Biological Chemistry, 1949