1cp7
AMINOPEPTIDASE FROM STREPTOMYCES GRISEUS
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OverviewOverview
SGAP is an aminopeptidase present in the extracellular fluid of, Streptomyces griseus cultures. It is a double-zinc enzyme with a strong, preference for large hydrophobic amino-terminus residues. It is a, monomeric (30 kDa) heat-stable enzyme, with a high and efficient catalytic, activity modulated by calcium ions. The small size, high activity and heat, stability make SGAP a very attractive enzyme for various biotechnological, applications. Only one other related aminopeptidase (Aeromonas, proteolytica AP; AAP) has been structurally analyzed to date and its, structure was shown to be considerably similar to SGAP, despite the low, sequence homology between the two enzymes. The motivation for the detailed, structural analysis of SGAP originated from a strong mechanistic interest, in the ... [(full description)]
About this StructureAbout this Structure
1CP7 is a [Single protein] structure of sequence from [Streptomyces griseus] with ZN and CA as [ligands]. Structure known Active Sites: ACT and CA. Full crystallographic information is available from [OCA].
ReferenceReference
Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 A resolution., Gilboa R, Greenblatt HM, Perach M, Spungin-Bialik A, Lessel U, Wohlfahrt G, Schomburg D, Blumberg S, Shoham G, Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):551-8. PMID:10771423
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