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Literature summary 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)

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Bos taurus
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bovine
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Reaction

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

Source Tissue

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

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