The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 4.3.2.5     
Accepted name: peptidylamidoglycolate lyase
Reaction: [peptide]-(2S)-2-hydroxyglycine = [peptide]-amide + glyoxylate
Other name(s): α-hydroxyglycine amidating dealkylase; peptidyl-α-hydroxyglycine α-amidating lyase; HGAD; PGL; PAL; peptidylamidoglycolate peptidylamide-lyase
Systematic name: [peptide]-(2S)-2-hydroxyglycine peptidyl-amide-lyase (glyoxylate-forming)
Comments: Requires zinc. The enzyme acts on the product of the reaction catalysed by EC 1.14.17.3 peptidylglycine monooxygenase, thus removing a terminal glycine residue and leaving a des-glycine peptide amide. In mammals, the two activities are part of a bifunctional protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 131689-50-4
References:
1.  Katapodis, A.G., Ping, D. and May, S.W. A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of α-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine α-amidating monooxygenase in peptide amidation. Biochemistry 29 (1990) 6115–6120. [PMID: 2207061]
2.  Bell, J., Ash, D.E., Snyder, L.M., Kulathila, R., Blackburn, N.J. and Merkler, D.J. Structural and functional investigations on the role of zinc in bifunctional rat peptidylglycine α-amidating enzyme. Biochemistry 36 (1997) 16239–16246. [PMID: 9405058]
[EC 4.3.2.5 created 1992, modified 2019]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald