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BRENDA support

Literature summary for 3.1.1.32 extracted from

  • Hiratsuka, S.; Kitagawa, T.; Yamagishi, K.; Wada, S.
    Phospholipase A1 activity of crude enzyme extracted from the ovaries of skipjack tuna (2008), Fish. Sci., 74, 146-152.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Katsuwonus pelamis
-
skipjack tuna
-

Source Tissue

Source Tissue Comment Organism Textmining
ovary PLA1 activity is predominant in the ovaries Katsuwonus pelamis
-
pyloric cecum
-
Katsuwonus pelamis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + H2O phosphatidylcholine is more easily hydrolyzed than phosphatidylethanolamine Katsuwonus pelamis 2-acylglycerophosphocholine + a fatty acid anion
-
?
phosphatidylethanolamine + H2O
-
Katsuwonus pelamis lysophosphatidylethanolamine + a fatty acid anion
-
?

Synonyms

Synonyms Comment Organism
phosphatidate 1-acylhydorolase
-
Katsuwonus pelamis
PLA1
-
Katsuwonus pelamis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 30
-
Katsuwonus pelamis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
-
approximately half of the activity remains at 0°C Katsuwonus pelamis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7
-
Katsuwonus pelamis