Aminopeptidase S

Aminopeptidase S (EC 3.4.11.24, Mername-AA022 peptidase, SGAP, aminopeptidase (Streptomyces griseus), Streptomyces griseus aminopeptidase, S. griseus AP, double-zinc aminopeptidase) is an enzyme.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues

This enzyme contains two zinc molecules in its active site and is activated by Ca²⁺.

References

↑ Spungin, A. and Blumberg, S. (1989). "Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme". Eur. J. Biochem. 183: 471–477. doi:10.1111/j.1432-1033.1989.tb14952.x. PMID 2503378.
↑ Ben-Meir, D., Spungin, A., Ashkenazi, R. and Blumberg, S. (1993). "Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution". Eur. J. Biochem. 212: 107–112. doi:10.1111/j.1432-1033.1993.tb17639.x. PMID 8444149.
↑ Arima, J., Uesugi, Y., Iwabuchi, M. and Hatanaka, T. (2006). "Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica". Appl. Microbiol. Biotechnol. 70: 541–547. doi:10.1007/s00253-005-0105-8. PMID 16080009.
↑ Fundoiano-Hershcovitz, Y., Rabinovitch, L., Langut, Y., Reiland, V., Shoham, G. and Shoham, Y. (2004). "Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus". FEBS Lett. 571: 192–196. doi:10.1016/j.febslet.2004.07.001. PMID 15280041.
↑ Gilboa, R., Greenblatt, H.M., Perach, M., Spungin-Bialik, A., Lessel, U., Wohlfahrt, G., Schomburg, D., Blumberg, S. and Shoham, G. (2000). "Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 Å resolution". Acta Crystallogr. D Biol. Crystallogr. 56: 551–558. doi:10.1107/s0907444900002420. PMID 10771423.

External links

Aminopeptidase S at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O

3.4.13	Dipeptidase 1 2 3

3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II

3.4.15	Angiotensin-converting enzyme

3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase

3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II

Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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