Serralysin

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Serralysin (EC 3.4.24.40, Pseudomonas aeruginosa alkaline proteinase, Escherichia freundii proteinase, Serratia marcescens extracellular proteinase, Serratia marcescens metalloproteinase, Pseudomonas aeruginosa alk. protease, Serratia marcescens metalloprotease) is an enzyme.^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8] This enzyme catalyses the following chemical reaction

Preferential cleavage of bonds with hydrophobic residues in P1'

This extracellular endopeptidase is present in Pseudomonas aeruginosa, Escherichia freundii, Serratia marcescens and Erwinia chrysanthemi.

References

↑ Morihara, K., Tsuzuki, H. and Oka, T. (1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Arch. Biochem. Biophys. 123 (3): 572–588. doi:10.1016/0003-9861(68)90179-3. PMID 4967801.
↑ Morihara, K., Tsuzuki, H. and Oka, T. (1973). "On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic peptides". Biochim. Biophys. Acta 309 (2): 414–429. doi:10.1016/0005-2744(73)90040-5. PMID 4199986.
↑ Nakajima, M., Mizusawa, K. and Yoshida, F. (1974). "Purification and properties of an extracellular proteinase of psychrophilic Escherichia freundii". Eur. J. Biochem. 44 (1): 87–96. doi:10.1111/j.1432-1033.1974.tb03460.x. PMID 4212288.
↑ Decedue, C.J., Broussard, E.A., II, L arson, A.D. and Braymer, H.D. (1979). "Purification and characterization of the extracellular proteinase of Serratia marcescens". Biochim. Biophys. Acta 569 (2): 293–301. doi:10.1016/0005-2744(79)90065-2. PMID 383155.
↑ Doerr, M. and Traub, W.H. (1984). "Purification and characterization of two Serratia marcescens proteases". Zentralbl. Bakteriol., Mikrobiol. Hyg. Ser. A 257 (1): 6–19. PMID 6380155.
↑ Nakahama, K., Yoshimura, K., Marumoto, R., Kikuchi, M., Lee, I.S., Hase, T. and Matsubara, H. (1986). "Cloning and sequencing of Serratia protease gene". Nucleic Acids Res. 14: 5843–5856. doi:10.1093/nar/14.14.5843. PMC 311595. PMID 3016665.
↑ Dahler, G.S., Barras, F. and Keen, N.T. (1990). "Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16". J. Bacteriol. 172 (10): 5803–5815. PMID 2211513.
↑ Okuda, K., Morihara, K., Atsumi, Y., Takeuchi, H., Kawamoto, S., Kawasaki, H., Suzuki, K. and Fukushima, J. (1990). "Complete nucleotide sequence of the structural gene for alkaline proteinase from Pseudomonas aeruginosa IFO 3455". Infect. Immun. 58 (12): 4083–4088. PMID 2123832.

External links

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

Proteases: metalloendopeptidases (EC 3.4.24)

ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13

Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28

Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

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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