Peptidylamidoglycolate lyase
| peptidylamidoglycolate lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.2.5 | ||||||||
| CAS no. | 131689-50-4 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, a peptidylamidoglycolate lyase (EC 4.3.2.5) is an enzyme that catalyzes the chemical reaction
- peptidylamidoglycolate peptidyl amide + glyoxylate
Hence, this enzyme has one substrate, , and two products, and glyoxylate.
This enzyme belongs to the family of lyases, specifically amidine lyases. The systematic name of this enzyme class is peptidylamidoglycolate peptidyl-amide-lyase (glyoxylate-forming). Other names in common use include alpha-hydroxyglycine amidating dealkylase, peptidyl-alpha-hydroxyglycine alpha-amidating lyase, HGAD, PGL, PAL, and peptidylamidoglycolate peptidylamide-lyase.
References[]
- Katopodis AG, Ping D, May SW (1990). "A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation". Biochemistry. 29 (26): 6115–20. doi:10.1021/bi00478a001. PMID 2207061.
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Categories:
- EC 4.3.2
- Enzymes of unknown structure
- Enzyme stubs