Ubiquitin—calmodulin ligase
ubiquitin-calmodulin ligase | |||||||||
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Identifiers | |||||||||
EC number | 6.3.2.21 | ||||||||
CAS number | 119632-60-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, an ubiquitin-calmodulin ligase (EC 6.3.2.21) is an enzyme that catalyzes the chemical reaction
- n ATP + calmodulin + n ubiquitin n AMP + n diphosphate + (ubiquitin)n-calmodulin
The 3 substrates of this enzyme are ATP, calmodulin, and ubiquitin, whereas its 3 products are AMP, diphosphate, and (ubiquitin)n-calmodulin.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is calmodulin:ubiquitin ligase (AMP-forming). Other names in common use include ubiquityl-calmodulin synthase, ubiquitin-calmodulin synthetase, ubiquityl-calmodulin synthetase, and uCaM-synthetase.
References
- Jennissen HP, Laub M (1988). "Ubiquitin-calmodulin conjugating activity from cardiac muscle". Biol. Chem. Hoppe-Seyler. 369 (12): 1325–30. PMID 2853950. doi:10.1515/bchm3.1988.369.2.1325.
- Ziegenhagen R, Jennissen HP (1988). "Multiple ubiquitination of vertebrate calmodulin by reticulocyte lysate and inhibition of calmodulin conjugation by phosphorylase kinase". Biol. Chem. Hoppe-Seyler. 369 (12): 1317–24. PMID 2853949. doi:10.1515/bchm3.1988.369.2.1317.
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