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: 100970635(PAM)
GGO: 101148887(PAM)
PON: 100449730(PAM)
NLE: 100603954(PAM)
MCC: 707733(PAM)
MCF: 101926659(PAM)
CSAB: 103244283(PAM)
RRO: 104669199(PAM)
RBB: 108527716(PAM)
CJC: 100396001(PAM)
SBQ: 101034151(PAM)
MMU: 18484(Pam)
RNO: 25508(Pam)
CGE: 100770162(Pam)
NGI: 103738185(Pam)
HGL: 101716909(Pam)
CCAN: 109689129(Pam) 109698017
OCU: 100352005(PAM)
TUP: 102499925(PAM)
CFA: 479145(PAM)
AML: 100484534(PAM)
UMR: 103656467(PAM)
ORO: 101383156(PAM)
FCA: 101084598(PAM)
PTG: 102961161(PAM)
AJU: 106982276(PAM)
BTA: 280890(PAM)
BOM: 102271872(PAM)
BIU: 109562372(PAM)
PHD: 102335695(PAM)
CHX: 102190130(PAM)
OAS: 101112815(PAM)
SSC: 100526040(PAM)
CFR: 102509591(PAM)
CDK: 105103083(PAM)
BACU: 103008694(PAM)
LVE: 103088789(PAM)
OOR: 101274063(PAM)
ECB: 791244(PAM)
EPZ: 103555847(PAM)
EAI: 106831159(PAM)
MYB: 102257709(PAM)
MYD: 102752613(PAM)
HAI: 109394174(PAM)
RSS: 109445511(PAM)
PALE: 102894575(PAM)
LAV: 100655604(PAM)
TMU: 101356870
MDO: 100030601(PAM)
OAA: 100073355(PAM)
GGA: 427274(PAM)
CJO: 107306340(PAM)
APLA: 101795983(PAM)
ACYG: 106043740(PAM)
TGU: 100227923(PAM)
GFR: 102039677(PAM)
FAB: 101821831(PAM)
PHI: 102114573(PAM)
PMAJ: 107215969(PAM)
CCW: 104693194(PAM)
FPG: 101920860(PAM)
FCH: 102052743(PAM)
CLV: 102087217(PAM)
EGZ: 104135057(PAM)
ASN: 102374229(PAM)
AMJ: 102559599(PAM)
PSS: 102462977(PAM)
CMY: 102946187(PAM)
CPIC: 101942761(PAM)
ACS: 100562563(pam)
PVT: 110079386(PAM)
PBI: 103055156(PAM) 103062674
GJA: 107121208(PAM)
XLA: 379207(pam.L) 397736(pam.S)
XTR: 100170159(pam)
NPR: 108797815(PAM)
DRE: 570822(pam)
SGH: 107558261(pam) 107560403
IPU: 108277198(pam)
AMEX: 103031431(pam)
TRU: 101062613(pam)
LCO: 104938829(pam) 104939677
NCC: 104955430
MZE: 101484633(pam)
OLA: 101164528(pam)
XMA: 102227462(pam)
PRET: 103473165(pam)
NFU: 107395057(pam)
CSEM: 103389193(pam)
LCF: 108877750(pam)
HCQ: 109530660(pam)
BPEC: 110161642(pam)
SASA: 106571984(pam)
ELS: 105020460(pam)
SFM: 108929922(pam)
LCM: 102348819(PAM)
CMK: 103178402(pam)
DME: Dmel_CG3832(Phm)
DSI: Dsimw501_GD24986(Dsim_GD24986)
MDE: 101895308
AAG: 5570501
AME: 412898
BIM: 100742180
BTER: 100644842
SOC: 105198561
AEC: 105152181
ACEP: 105625891
HST: 105188766
CFO: 105248300
LHU: 105677788
PGC: 109858237
NVI: 100114893
TCA: 664519
DPA: 109533856
NVL: 108560955
BMOR: 101742277
PMAC: 106716851
PRAP: 110993134
PXY: 105388351
API: 100161384
DNX: 107173105
ZNE: 110835112
TUT: 107370625
CEL: CELE_T19B4.1(pamn-1) CELE_Y71G12B.4(pghm-1)
TSP: Tsp_08244
OBI: 106870427
LAK: 106162187
EGL: EGR_00446
ADF: 107333635
HMG: 100212498
AQU: 100636212
OLU: OSTLU_15206(PAM1)
APRO: F751_4456
RDE: RD1_2432(pam)
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 298:686-8 (1982)
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 169:579-84 (1987)
DOI:10.1111/j.1432-1033.1987.tb13648.x
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 241:673-83 (1985)
DOI:10.1016/0003-9861(85)90594-6
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 29:6115-20 (1990)
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 1:290-9 (1987)
DOI:10.1210/mend-1-4-290
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 261:1815-22 (1986)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.17.3
IUBMB Enzyme Nomenclature: 1.14.17.3
ExPASy - ENZYME nomenclature database: 1.14.17.3
BRENDA, the Enzyme Database: 1.14.17.3
CAS: 90597-47-0

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