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Literature summary for 3.6.1.7 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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Oryctolagus cuniculus enzyme thought to participate in the regulation of glycolytic pathways and the synthesis of pyrimidine ?
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal muscle Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
monomer
-
Oryctolagus cuniculus