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Literature summary extracted from

  • Saudek, V.; Williams, R.J.P.
    Secondary structure of acylphosphatase from rabbit skeletal muscle. A nuclear magnetic resonance study [published erratum appears in J Mol Biol 1988 Oct 5;203(3):835] (1988), J. Mol. Biol., 199, 233-237.
    View publication on PubMed

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 Oryctolagus cuniculus enzyme thought to participate in the regulation of glycolytic pathways and the synthesis of pyrimidine ?
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?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7
-
Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 muscle skeletal muscle Oryctolagus cuniculus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Oryctolagus cuniculus carboxylate + phosphate
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?
3.6.1.7 additional information enzyme thought to participate in the regulation of glycolytic pathways and the synthesis of pyrimidine Oryctolagus cuniculus ?
-
?

Subunits

EC Number Subunits Comment Organism
3.6.1.7 monomer
-
Oryctolagus cuniculus