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Literature summary for 3.6.1.7 extracted from

  • Thunnissen, M.M.; Taddei, N.; Liguri, G.; Ramponi, G.; Nordlund, P.
    Crystal structure of common type acylphosphatase from bovine testis (1997), Structure, 5, 69-79.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
common-type enzyme, resolution of 1.8 A Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bos taurus enzyme is thought to regulate metabolic processes in which acylphosphates are involved, such as glycolysis and production of ribonucleotides ?
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
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bovine
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Reaction

Reaction Comment Organism Reaction ID
an acylphosphate + H2O = a carboxylate + phosphate reaction mechanism Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
testis common type enzyme Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O phospho-aspartyl intermediate Bos taurus ?
-
?
acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Bos taurus carboxylate + phosphate
-
?
additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Bos taurus ?
-
?
additional information hydrolyzes specific only acylphosphates Bos taurus ?
-
?
additional information specific phosphomonohydrolase activity Bos taurus ?
-
?
additional information enzyme is thought to regulate metabolic processes in which acylphosphates are involved, such as glycolysis and production of ribonucleotides Bos taurus ?
-
?