KEGG   ENZYME: 1.14.17.3
Entry
EC 1.14.17.3                Enzyme                                 

Name
peptidylglycine monooxygenase;
peptidylglycine 2-hydroxylase;
peptidyl alpha-amidating enzyme;
peptide-alpha-amide synthetase;
peptide alpha-amidating enzyme;
peptide alpha-amide synthase;
peptidylglycine alpha-hydroxylase;
peptidylglycine alpha-amidating monooxygenase;
PAM-A;
PAM-B;
PAM;
peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
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
Sysname
[peptide]-glycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
Reaction(IUBMB)
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O [RN:R03912]
Reaction(KEGG)
R03912
Substrate
[peptide]-glycine [CPD:C02303];
ascorbate [CPD:C00072];
O2 [CPD:C00007]
Product
[peptide]-(2S)-2-hydroxyglycine [CPD:C03303];
monodehydroascorbate [CPD:C01041];
H2O [CPD:C00001]
Comment
A copper protein. The enzyme binds two copper ions with distinct roles during catalysis. 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. In mammals, the two activities are part of a bifunctional protein. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
History
EC 1.14.17.3 created 1989, modified 2019
Orthology
K00504  peptidylglycine monooxygenase
K24006  peptidylglycine monooxygenase / peptidylamidoglycolate lyase
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)
MCAL: 110305227(Pam)
MPAH: 110321660(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)
VVP: 112915565(PAM)
AML: 100484534(PAM)
UMR: 103656467(PAM)
UAH: 113255028(PAM)
ORO: 101383156(PAM)
ELK: 111148403
FCA: 101084598(PAM)
PTG: 102961161(PAM)
PPAD: 109267636(PAM)
AJU: 106982276(PAM)
BTA: 280890(PAM)
BOM: 102271872(PAM)
BIU: 109562372(PAM)
BBUB: 102409727(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)
DLE: 111183960(PAM)
PCAD: 102993897(PAM)
ECB: 791244(PAM)
EPZ: 103555847(PAM)
EAI: 106831159(PAM)
MYB: 102257709(PAM)
MYD: 102752613(PAM)
MNA: 107544178(PAM)
HAI: 109394174(PAM)
DRO: 112307140(PAM)
PALE: 102894575(PAM)
RAY: 107509145(PAM)
MJV: 108391703(PAM)
LAV: 100655604(PAM)
TMU: 101356870
MDO: 100030601(PAM)
SHR: 100929728(PAM)
PCW: 110199219(PAM)
OAA: 100073355(PAM)
GGA: 427274(PAM)
CJO: 107306340(PAM)
NMEL: 110389678(PAM)
APLA: 101795983(PAM)
ACYG: 106043740(PAM)
TGU: 100227923(PAM)
LSR: 110477851(PAM)
SCAN: 103822855(PAM)
GFR: 102039677(PAM)
FAB: 101821831(PAM)
PHI: 102114573(PAM)
PMAJ: 107215969(PAM)
CCAE: 111940620(PAM)
CCW: 104693194(PAM)
ETL: 114064047(PAM)
FPG: 101920860(PAM)
FCH: 102052743(PAM)
CLV: 102087217(PAM)
EGZ: 104135057(PAM)
NNI: 104010298(PAM)
ACUN: 113489698(PAM)
PADL: 103920863(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)
TSR: 106548589(PAM)
PMUA: 114606841(PAM)
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)
PHYP: 113543505(pam)
AMEX: 103031431(pam)
EEE: 113576732(pam)
TRU: 101062613(pam)
LCO: 104938829(pam)
MZE: 101484633(pam)
ONL: 100700800(pam)
OLA: 101164528(pam)
XMA: 102227462(pam)
XCO: 114149523(pam)
PRET: 103473165(pam)
CVG: 107098487(pam)
NFU: 107395057(pam)
KMR: 108246466(pam)
ALIM: 106522199(pam)
AOCE: 111579145(pam)
CSEM: 103389193(pam)
POV: 109637635(pam)
LCF: 108877750(pam)
SDU: 111221118(pam)
SLAL: 111659622(pam)
HCQ: 109530660(pam)
BPEC: 110161642(pam)
MALB: 109960744(pam)
SASA: 106571984(pam)
OTW: 112219988(pam)
SALP: 111961960(pam)
ELS: 105020460(pam)
SFM: 108929922(pam)
PKI: 111835769(pam)
LCM: 102348819(PAM)
CMK: 103178402(pam)
RTP: 109919477(pam)
APLC: 110987818
DME: Dmel_CG3832(Phm)
DER: 6548056
DSE: 6615827
DSI: Dsimw501_GD24986(Dsim_GD24986)
DAN: 6494903
DSR: 110191555
DPE: 6591044
DWI: 6637882
DAZ: 108616319
DNV: 115564826
DHE: 111600106
DVI: 6625978
MDE: 101895308
LCQ: 111678022
AAG: 5570501
AALB: 109413127
AME: 412898
BIM: 100742180
BTER: 100644842
CCAL: 108626394
OBB: 114872670
SOC: 105198561
MPHA: 105834205
AEC: 105152181
ACEP: 105625891
PBAR: 105431355
VEM: 105559346
HST: 105188766
DQU: 106747041
CFO: 105248300
LHU: 105677788
PGC: 109858237
OBO: 105277440
PCF: 106786055
CSOL: 105366100
MDL: 103573620
TCA: 664519
DPA: 109533856
ATD: 109600562
NVL: 108560955
BMOR: 101742277
BMAN: 114244909
PMAC: 106716851
PRAP: 110993134
HAW: 110383814
TNL: 113496548
PXY: 105388351
API: 100161384
DNX: 107173105
RMD: 113552161
BTAB: 109039943
CLEC: 106666670
ZNE: 110835112
TUT: 107368260
CEL: CELE_T19B4.1(pamn-1) CELE_Y71G12B.4(pghm-1)
PCAN: 112553876
MYI: 110443164
OBI: 106870427
LAK: 106162187
SHX: MS3_06043
EGL: EGR_00446
ADF: 107333635
AQU: 100636212
APRO: F751_4456
OLU: OSTLU_15206(PAM1)
 » show all
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)
DOI:10.1038/298686a0
Reference
2  [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
3  [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)
Reference
4  [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
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: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)
DOI:10.1021/bi00478a001
Reference
7  [PMID:9360928]
  Authors
Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM
  Title
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
  Journal
Science 278:1300-5 (1997)
DOI:10.1126/science.278.5341.1300
Reference
8  [PMID:15131304]
  Authors
Prigge ST, Eipper BA, Mains RE, Amzel LM
  Title
Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex.
  Journal
Science 304:864-7 (2004)
DOI:10.1126/science.1094583
Reference
9  [PMID:20958070]
  Authors
Chufan EE, Prigge ST, Siebert X, Eipper BA, Mains RE, Amzel LM
  Title
Differential reactivity between two copper sites in peptidylglycine alpha-hydroxylating monooxygenase.
  Journal
J Am Chem Soc 132:15565-72 (2010)
DOI:10.1021/ja103117r
Reference
10 [PMID:26982589]
  Authors
Chauhan S, Hosseinzadeh P, Lu Y, Blackburn NJ
  Title
Stopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated  Electron Transfer Pathway in Peptidylglycine Monooxygenase.
  Journal
Biochemistry 55:2008-21 (2016)
DOI:10.1021/acs.biochem.6b00061
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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