Biology:Staphopain

Staphopain (EC 3.4.22.48, staphylopain) is an enzyme.^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates.

This enzyme is present in several species of Staphylococcus.

References

↑ Hofmann, B.; Hecht, H.J.; Kiess, M.; Schomburg, D. (1993). "Crystal structure of a thiol proteinase from Staphylococcus aureus V8 in the E-64 inhibitor complex". Acta Crystallographica Section A 49: c102. doi:10.1107/s0108767378097081.
↑ "Staphylopain". Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. 1998. pp. 669–671.
↑ "Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis". Biological Chemistry 382 (11): 1575–82. November 2001. doi:10.1515/bc.2001.192. PMID 11767947.

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

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v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)