Barrierpepsin
Appearance
Barrierpepsin | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.23.35 | ||||||||
CAS no. | 152060-38-3 | ||||||||
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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Barrierpepsin (EC 3.4.23.35, barrier proteinase, Bar proteinase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Selective cleavage of -Leu6-Lys- bond in the pheromone alpha-mating factor
This endopeptidase is present in baker's yeast (Saccharomyces cerevisiae).
References
[edit]- ^ MacKay VL, Welch SK, Insley MY, Manney TR, Holly J, Saari GC, Parker ML (January 1988). "The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin". Proceedings of the National Academy of Sciences of the United States of America. 85 (1): 55–9. Bibcode:1988PNAS...85...55M. doi:10.1073/pnas.85.1.55. PMC 279480. PMID 3124102.
- ^ MacKay VL, Armstrong J, Yip C, Welch S, Walker K, Osborn S, Sheppard P, Forstrom J (1991). "Characterization of the Bar Proteinase, an Extracellular Enzyme from the Yeast Saccharomyces Cerevisiae". Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology. Vol. 306. pp. 161–72. doi:10.1007/978-1-4684-6012-4_21. ISBN 978-1-4684-6014-8. PMID 1812704.
External links
[edit]- Barrierpepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)