Fructose-1,6-bisphosphate aldolase from Vibrio marinus, a psychrophilic marine bacterium

✍ Scribed by L. P. Jones; Dr. R. Y. Morita; R. R. Becker

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 607 KB
• Volume: 19
• Category: Article
• ISSN: 0233-111X
• DOI: 10.1002/jobm.19790190205

✦ Synopsis

Fructosr-1,6-bispliosphate aldolase (Pru-P,A) from a psychrophilic marine bacterium n a s found to be Class 11 aldolase based on activation by I<+, activation by divaleiit cations, iiiartivatioii by EDTA, low molecular weight. and similar values for K , , I'II~~x, and ARRIIENIUS activation energy. This enzyme was not markedly different in aniino acid composition froni the enzymes froni nicsophilic arid theriiiophihc organisms, yet i t has unusual thermal properties.

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Fructose l,(j-bisphospliate aldolase ( F ~L I -P ~A )

is the enxynic in the EMBDEN-MEYERHOF pathway v hich catalyzes the rcversible aldol condensation between dihydroxyacetone phosphate (DHAP) arid glycernldehyde 3-phosphate (GAP). Aldolases are found t o be of two types which do not appear to be phylogenctically related. Class I aldolases are typically found in plants, protozoa, and green algae ( L~UTTER 1Y(j5), are tetranieric with a molecular weight of 150,000 (MARTIN and AMES 1961), do not require the presence of a metal ion for activity (CHRISTIAN and WARBURG 1955, KUTTER and LING 1958, WESTHEAD c t u l . l W 3 ) , and are not inactivated in the presence of high levels of ethylene dianiine tetraacetic acid (EDTA) I ) Published as technical paper no. 5045, Oregon Agricultural Experiment Station.