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IUBMB Comments The enzyme has been characterized from the bacteria Streptomyces griseus , Streptomyces naraensis , and Streptomyces cacaoi . Specificity is similar to that of thermolysin, but the enzyme is much more sensitive to inhibition by sulfanylacetyl-Phe-Leu. Little structural similarity to other bacterial metalloendopeptidases. Type example of peptidase family M5 .
Reaction Schemes
Preferential cleavage of bonds with hydrophobic residues in P1'
Synonyms
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EC 3.4.24.4
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formerly
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Neutral metalloproteinase
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Pronase component
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Streptomyces griseus neutral proteinase
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Preferential cleavage of bonds with hydrophobic residues in P1'
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hydrolysis of peptide bond
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azocasein + H2O
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Substrates: -
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furylacryloyl-Gly-Leu-NH2 + H2O
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Substrates: -
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Oxidized insulin B-chain + H2O
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Substrates: cleavage at: Phe1-Val2, His5-Leu6, His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Leu17-Val18, Gly23-Phe24, Phe24-Phe25, Phe25-Tyr26
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additional information
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Substrates: specificity overview: synthetic peptides
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casein + H2O
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Substrates: -
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casein + H2O
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Substrates: -
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Zinc
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contains 1 gatom of zinc per mol of enzyme
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2-mercaptoacetyl-L-Leu-D-Phe
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weak
2-mercaptoacetyl-L-Leu-L-Phe
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2-mercaptoacetyl-L-Phe-L-Leu
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much more sensitive to inhibition than thermolysin
additional information
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not inhibited by PMSF and iodoacetamide
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EDTA
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EDTA
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10 mM inactivates activity almost completely, addition of 1 mM Zn2+, Co2+ or Mn2+ can restore depressed activity to 100, 142 and 115% respectively
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YM15
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brenda
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brenda
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brenda
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brenda
YM15
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brenda
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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MYCO_STRCI
550
1
58678
Swiss-Prot
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37100
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Streptomyces naraensis, gel filtration, sedimentation-diffusion method, sedimentation-viscosity method, amino acid composition
60000
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Streptomyces cacaoi, calculation from nucleotide sequence of the cloned gene
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glycoprotein
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contains 1.86% of carbohydrate, with complete absence of hexosamine and sialic acid
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additional information
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mutations in the hydrophobic region or in the proline at the boundary of the hydrophobic core-cleavage region delay export of the enzyme and reduce total secretion by a factor of 2-10
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by acetone precipitation and Fractogel CM-650 chromatography
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expressed in Streptomyces lividans
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in Streptomyces lividans using a pIJ702 vector
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Morihara, K.; Tsuzuki, H.; Oka, T.
Comparison of the specificities of various neutral proteinases from microorganisms
Arch. Biochem. Biophys.
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572-588
1968
Streptomyces griseus
brenda
Chang, P.C.; Kuo, T.C.; Tsugita, A.; Wu Lee, Y.H.W.
Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product
Gene
88
87-95
1990
Streptomyces cacaoi, Streptomyces cacaoi YM15
brenda
Blumberg, S.; Tauber, Z.
Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides
Eur. J. Biochem.
136
151-154
1983
Streptomyces griseus
brenda
Hiramatsu, A.; Ouchi, T.
A neutral proteinase from Streptomyces naraensis. 3. An improved purification and some physiochemical properties
J. Biochem.
71
767-781
1972
Streptomyces naraensis
brenda
Ishii, S.; Kumazaki, T.
Mycolysin
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
412-413
2004
Streptomyces cacaoi
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brenda
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