Fructose-1,6-bisphosphate aldolase fromVibrio marinus, a psychrophilic marine bacterium
- 1 January 1979
- journal article
- Published by Wiley in Journal of Basic Microbiology
- Vol. 19 (2) , 97-106
- https://doi.org/10.1002/jobm.3630190205
Abstract
Fructose-1,6-bisphosphate aldolase (Fru-P2A) from a psychrophilic marine bacterium was found to be Class II aldolase based on activation by K+, activation by divalent cations, inactivation by EDTA, low molecular weight, and similar values for Km, Vmax, and Arrhenius activation energy. This enzyme was not markedly different in amino acid composition from the enzymes from mesophilic and thermophilic organisms, yet it has unusual thermal properties.Keywords
This publication has 25 references indexed in Scilit:
- Oxygen-18 studies of the mechanisms of yeast and muscle aldolasesBiochemistry, 1974
- Fructose-1,6-diphosphate aldolase from Lactobacillus caseiArchives of Biochemistry and Biophysics, 1974
- Functional role of metal ions in a class II aldolaseBiochemistry, 1969
- On the average hydrophobicity of proteins and the relation between it and protein structureJournal of Theoretical Biology, 1967
- Fructose 1,6-diphosphate aldolase of Candida utilis: Purification and propertiesArchives of Biochemistry and Biophysics, 1966
- The correlation between molecular weight and elution behaviour in the gel chromatography of proteinsJournal of Chromatography A, 1966
- REISOLATION AND EMENDATION OF DESCRIPTION OFVIBRIO MARINUS(RUSSELL) FORDJournal of Bacteriology, 1964
- The relative thermostability of cytoplasmic proteins from thermophilic bacteriaArchives of Biochemistry and Biophysics, 1957
- [40] Aldolase from yeastPublished by Elsevier ,1955
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934