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Literature summary for 3.4.23.32 extracted from

  • Fujinaga, M.; Cherney, M.M.; Oyama, H.; Oda, K.; James, M.N.
    The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum (2004), Proc. Natl. Acad. Sci. USA, 101, 3364-3369.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme complexed with angiotensin II, hanging drop method, room temperature, from 42% saturated ammonium sulfate, 0.1 M sodium acetate, pH 4.0, 10% v/v ethylene glycol, crystals are soaked in cryosolution containing 30% glvcerol, 45% saturated ammonium sulfate,and 0.1 M sodium acetate, pH 4.0, heavy atom derivatizing, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution, molecular modeling and multiple isomorphous replacement phasing Scytalidium lignicola

Organism

Organism UniProt Comment Textmining
Scytalidium lignicola
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Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of proteins with broad specificity, cleaving Phe24-/-Phe, but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin active site structure and substrate binding structure and mechanism, hydrolysis mechanism Scytalidium lignicola

Subunits

Subunits Comment Organism
More molecular structure analysis Scytalidium lignicola

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the eqolisin family of proteases Scytalidium lignicola
SCP-B
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Scytalidium lignicola
Scytalidium lignicolum pepstatin-insensitive carboxyl peptidase
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Scytalidium lignicola