Beta-lytic metalloendopeptidase (EC 3.4.24.32, Myxobacter beta-lytic proteinase, achromopeptidase component, beta-lytic metalloproteinase, beta-lytic protease, Myxobacterium sorangium beta-lytic proteinase, Myxobacter495 beta-lytic proteinase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
Beta-lytic metalloendopeptidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.24.32 | ||||||||
CAS no. | 37288-92-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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- Cleavage of N-acetylmuramoyl-Ala, and of the insulin B chain at Gly23-Phe > Val18-Cya
This enzyme is present in Achromobacter lyticus and Lysobacter enzymogenes.
References
edit- ^ Whitaker DR, Roy C, Tsai CS, Jurásek L (December 1965). "Lytic enzymes of Sorangium sp. A comparison of the proteolytic properties of the alpha- and beta-lytic proteases". Canadian Journal of Biochemistry. 43 (12): 1961–70. doi:10.1139/o65-219. PMID 5880182.
- ^ Whitaker DR, Roy C (June 1967). "Concerning the nature of the alpha- and beta-lytic proteases of Sorangium sp". Canadian Journal of Biochemistry. 45 (6): 911–6. doi:10.1139/o67-101. PMID 6034704.
- ^ Li SL, Norioka S, Sakiyama F (November 1990). "Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus". Journal of Bacteriology. 172 (11): 6506–11. doi:10.1128/jb.172.11.6506-6511.1990. PMC 526839. PMID 2228973.
External links
edit- Beta-lytic+metalloendopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)