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Literature summary for 4.3.2.5 extracted from

  • Husten, E.J.; Eipper, B.A.
    The membrane-bound bifunctional peptidylglycine alpha-amidating monooxygenase protein. Exploration of its domain structure through limited proteolysis. (1991), J. Biol. Chem., 266, 17004-17010.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
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Rattus norvegicus 16020
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Sprague-Dawley, EC 1.14.17.3 (PHM) and EC 4.3.2.5 (PAL) are part of a bifunctional, integral membrane protein precursor, peptidylglycine alpha-amidating monooxygenase, PAM, which consists of independent catalytic domains separated from each other and from the putative transmembrane domain by flexible regions accessible to attack by a wide variety of endoproteinases
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Source Tissue

Source Tissue Comment Organism Textmining
atrium
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Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha-acetyl-Tyr-Val-alpha-hydroxyglycine
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Rattus norvegicus Nalpha-acetyl-Tyr-Val-NH2 + glyoxylate
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?

Synonyms

Synonyms Comment Organism
PAL
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Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Rattus norvegicus