Phosphofructokinase in the mantle of the sea musselMytilus galloprovincialis Lmk.

✍ Scribed by Villamarin, J. A. ;Rodriguez-Torres, A. M. ;Ibarguren, I. ;Ramos-Martinez, J. I.

• Publisher: John Wiley and Sons
• Year: 1990
• Tongue: English
• Weight: 753 KB
• Volume: 255
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/jez.1402550304

✦ Synopsis

Abstract

Phosphofructokinase (PFK) from the mantle of Mytilus galloprovincialis Lmk. was purified 302‐fold with a yield of 27%. The enzyme proved to be a 340,000‐dalton oligomer comprising four identical 85,000‐dalton subunits.

Like other phosphofructokinases, the enzyme behaved cooperatively with fructose 6‐phosphate and was inhibited by high concentrations of ATP.

The fall in pH value produces a decrease of enzyme affinity for Fru 6‐P and for the activator AMP, together with a greater inhibition by ATP.

AMP, cyclic AMP, and fructose 2,6‐bisphosphate increased the affinity of mussel mantle PFK for Fru 6‐P and decreased the inhibition by ATP, while ammonium ions activated the enzyme increasing only the Vmax. Phospho__enol__pyruvate acted as an inhibitor, decreasing the affinity of the enzyme for Fru 6‐P.