A highly active alkaline phosphatase from the marine bacterium cobetia.
An alkaline phosphatase with unusually high specific activity has been found to be produced by the marine bacterium Cobetia marina (strain KMM MC-296) isolated from coelomic liquid of the mussel Crenomytilus grayanus. The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg of protein), no activation with divalent cations, resistance to high concentrations of inorganic phosphorus, as well as substrate specificity toward 5' nucleotides suggest that the enzyme falls in an intermediate position between unspecific alkaline phosphatases (EC 3.1.3.1) and 5' nucleotidases (EC 3.1.3.5).
Yu Plisova
E
E
Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, Vladivostok-22, 690022, Russia.
Balabanova
L A
LA
Ivanova
E P
EP
Kozhemyako
V B
VB
Mikhailov
V V
VV
Agafonova
E V
EV
Rasskazov
V A
VA
D015720:5'-Nucleotidase / Q000302:isolation & purification*; D000469:Alkaline Phosphatase / Q000302:isolation & purification*; D000818:Animals; D044129:Halomonadaceae / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D049879:Mytilidae / Q000382:microbiology*; D010140:Pacific Ocean; D013379:Substrate Specificity
D000469:Alkaline Phosphatase; D015720:5'-Nucleotidase