KEGG   ENZYME: 3.4.24.32Help
Entry
EC 3.4.24.32                Enzyme                                 

Name
beta-lytic metalloendopeptidase;
Myxobacter beta-lytic proteinase;
achromopeptidase component;
beta-lytic metalloproteinase;
beta-lytic protease;
Myxobacterium sorangium beta-lytic proteinase;
Myxobacter495 beta-lytic proteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage of N-acetylmuramoyl!Ala, and of the insulin B chain at Gly23!Phe > Val18!Cya
Comment
From Achromobacter lyticus and Lysobacter enzymogenes. Digests bacterial cell walls. Type example of peptidase family M23.
History
EC 3.4.24.32 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.32
Orthology
K20749  beta-lytic metalloendopeptidase
Genes
LAB: LA76x_3114
LCP: LC55x_0945
LGU: LG3211_0883
LEZ: GLE_0833
Taxonomy
Reference
1  [PMID:5880182]
  Authors
Whitaker DR, Roy C, Tsai CS, Jurasek L.
  Title
Lytic enzymes of Sorangium sp. A comparison of the proteolytic properties of the alpha- and beta-lytic proteases.
  Journal
Can J Biochem 43:1961-70 (1965)
Reference
2  [PMID:6034704]
  Authors
Whitaker DR, Roy C.
  Title
Concerning the nature of the alpha- and beta-lytic proteases of Sorangium sp.
  Journal
Can J Biochem 45:911-6 (1967)
Reference
3  [PMID:2228973]
  Authors
Li SL, Norioka S, Sakiyama F.
  Title
Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus.
  Journal
J Bacteriol 172:6506-11 (1990)
DOI:10.1128/JB.172.11.6506-6511.1990
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.4.24.32
IUBMB Enzyme Nomenclature: 3.4.24.32
ExPASy - ENZYME nomenclature database: 3.4.24.32
BRENDA, the Enzyme Database: 3.4.24.32
CAS: 37288-92-9

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