C-terminal processing peptidase (EC 3.4.21.102, CtpA gene product (Synechocystis sp.), photosystem II D1 protein processing peptidase, protease Re, tail-specific protease, Tsp protease) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
C-terminal processing peptidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.21.102 | ||||||||
CAS no. | 92480-11-0&title= 216484-75-2, 92480-11-0 | ||||||||
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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- The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala!Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C-terminal extension of the X1 polypeptide of photosystem II
Proteolytic processing of the X1 protein of photosystem II enables light-driven assembly of the tetranuclear manganese cluster.
See also
edit- D1 protein, also known as PsbA
References
edit- ^ Keiler KC, Sauer RT (1998). "Tsp protease". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 460–461.
- ^ Beebe KD, Shin J, Peng J, Chaudhury C, Khera J, Pei D (March 2000). "Substrate recognition through a PDZ domain in tail-specific protease". Biochemistry. 39 (11): 3149–55. doi:10.1021/bi992709s. PMID 10715137.
- ^ Liao DI, Qian J, Chisholm DA, Jordan DB, Diner BA (September 2000). "Crystal structures of the photosystem II D1 C-terminal processing protease". Nature Structural Biology. 7 (9): 749–53. doi:10.1038/78973. PMID 10966643.
External links
edit- C-terminal+processing+peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)