EC 3.4.21.100 - Sedolisin

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IntEnz Enzyme Nomenclature
EC 3.4.21.100

Names

Accepted name:
sedolisin
Other names:
Pseudomonas sp. pepstatin-insensitive carboxyl proteinase
pseudomonapepsin
pseudomonalisin
sedolysin
Systematic name:
-

Reaction

Comments:

An enzyme secreted by Pseudomonas sp. No. 101. Optimum pH is 4. It is distinguished from EC 3.4.21.101, xanthomonalisin, by its insensitivity to EPNP and from EC 3.4.23.31, scytalidopepsin B, by this property and by its unrelated amino-acid sequence. Inhibited by tyrostatin, a peptide aldehyde [2]. Type example of peptidase family S53.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Oda, K., Sugitani, M., Fukuhara, K. and Murao, S.
    Purification and properties of a pepstatin-insensitive carboxyl proteinase from a Gram-negative bacterium.
    Biochim. Biophys. Acta 923: 463-469 (1987). [PMID: 3548827]
  2. Oda, K., Nakatani, H. and Dunn, B.M.
    Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101.
    Biochim. Biophys. Acta 1120: 208-214 (1992). [PMID: 1562589]
  3. Wlodawer, A., Li, M., Dauter, Z., Gustchina, A., Uchida, K., Oyama, H., Dunn, B.M. and Oda, K.
    Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes.
    Nat. Struct. Biol. 8: 442-446 (2001). [PMID: 11323721]
  4. Wlodawer, A., Li, M., Gustchina, A., Oyama, H., Dunn, B.M. and Oda, K.
    Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
    Acta Biochim. Pol. 50: 81-102 (2003). [PMID: 12673349]

[EC 3.4.21.100 created 1995 as EC 3.4.23.37, transferred 2001 to EC 3.4.21.100, modified 2003]