1tkh

Structural highlights

Function

APX_STRGG An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).^{[1] [2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Aminopeptidase 3D structures
• Streptomyces griseus Aminopeptidase (SGAP)

References

1. ↑ Spungin A, Blumberg S. Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme. Eur J Biochem. 1989 Aug 1;183(2):471-7. PMID:2503378 doi:10.1111/j.1432-1033.1989.tb14952.x
2. ↑ Ben-Meir D, Spungin A, Ashkenazi R, Blumberg S. Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution. Eur J Biochem. 1993 Feb 15;212(1):107-12. PMID:8444149 doi:10.1111/j.1432-1033.1993.tb17639.x
3. ↑ Maras B, Greenblatt HM, Shoham G, Spungin-Bialik A, Blumberg S, Barra D. Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases. Eur J Biochem. 1996 Mar 15;236(3):843-6. PMID:8665903 doi:10.1111/j.1432-1033.1996.00843.x