KEGG   ENZYME: 1.14.17.3Help
Entry
EC 1.14.17.3                Enzyme                                 

Name
peptidylglycine monooxygenase;
peptidylglycine 2-hydroxylase;
peptidyl alpha-amidating enzyme;
peptide-alpha-amide synthetase;
synthase, peptide alpha-amide;
peptide alpha-amidating enzyme;
peptide alpha-amide synthase;
peptidylglycine alpha-hydroxylase;
peptidylglycine alpha-amidating monooxygenase;
PAM-A;
PAM-B;
PAM
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
Reaction(IUBMB)
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O [RN:R03912]
Reaction(KEGG)
Substrate
peptidylglycine [CPD:C02303];
ascorbate [CPD:C00072];
O2 [CPD:C00007]
Product
peptidyl(2-hydroxyglycine) [CPD:C03303];
dehydroascorbate [CPD:C05422];
H2O [CPD:C00001]
Comment
A copper protein. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
History
EC 1.14.17.3 created 1989
Orthology
K00504  
peptidylglycine monooxygenase
Genes
HSA: 
5066(PAM)
PTR: 
461974(PAM)
PPS: 
GGO: 
PON: 
MCC: 
707733(PAM)
MCF: 
MMU: 
18484(Pam)
RNO: 
25508(Pam)
CGE: 
HGL: 
TUP: 
CFA: 
479145(PAM)
AML: 
FCA: 
PTG: 
BTA: 
280890(PAM)
BOM: 
PHD: 
CHX: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
791244(PAM)
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
427274(PAM)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XLA: 
379207(pam-a) 397736(pam-b)
XTR: 
DRE: 
570822(pam)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
AGA: 
AAG: 
CQU: 
AME: 
408568(GB17423) 412898(Phm)
NVI: 
API: 
ISC: 
CEL: 
CBR: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
CRE: 
VCN: 
OLU: 
OTA: 
MIS: 
MPP: 
BPG: 
CSL: 
CVR: 
EHX: 
RDE: 
RBA: 
RB9882(pam)
 » show all
Taxonomy
Reference
1  [PMID:7099265]
  Authors
Bradbury AF, Finnie MD, Smyth DG.
  Title
Mechanism of C-terminal amide formation by pituitary enzymes.
  Journal
Nature. 298 (1982) 686-8.
Reference
2  [PMID:3691506]
  Authors
Bradbury AF, Smyth DG.
  Title
Enzyme-catalysed peptide amidation. Isolation of a stable intermediate formed by reaction of the amidating enzyme with an imino acid.
  Journal
Eur. J. Biochem. 169 (1987) 579-84.
  Organism
Sus scofa
Reference
3  [PMID:2994573]
  Authors
Glembotski CC.
  Title
Further characterization of the peptidyl alpha-amidating enzyme in rat anterior pituitary secretory granules.
  Journal
Arch. Biochem. Biophys. 241 (1985) 673-83.
  Organism
Rattus norvegicus
Reference
4  [PMID:2207061]
  Authors
Katopodis AG, Ping D, May SW.
  Title
A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation.
  Journal
Biochemistry. 29 (1990) 6115-20.
  Organism
Bos taurus
Reference
5  [PMID:3453894]
  Authors
Murthy AS, Keutmann HT, Eipper BA.
  Title
Further characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary.
  Journal
Mol. Endocrinol. 1 (1987) 290-9.
  Organism
Bos taurus
Reference
6  [PMID:3944110]
  Authors
Murthy AS, Mains RE, Eipper BA.
  Title
Purification and characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary.
  Journal
J. Biol. Chem. 261 (1986) 1815-22.
  Organism
Bos taurus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
90597-47-0

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