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
HSA5066(PAM)
PTR461974(PAM)
PPS100970635(PAM)
GGO101148887(PAM)
PON100449730(PAM)
NLE100603954(PAM)
MCC707733(PAM)
MCF101926659(PAM)
CSAB103244283(PAM)
CATY105576668(PAM)
PANU101026672(PAM)
TGE112626915(PAM)
RRO104669199(PAM)
RBB108527716(PAM)
TFN117064857(PAM)
PTEH111542665(PAM)
CJC100396001(PAM)
SBQ101034151(PAM)
CSYR103263009(PAM)
MMUR105875983(PAM)
OGA100956802(PAM)
MMU18484(Pam)
MCAL110305227(Pam)
MPAH110321660(Pam)
RNO25508(Pam)
MCOC116088825(Pam)
MUN110540758(Pam) 110540935 110543689
CGE100770162(Pam)
PLEU114699806(Pam)
NGI103738185(Pam)
HGL101716909(Pam)
CPOC100713254(Pam)
CCAN109689129(Pam) 109698017
DORD105989825(Pam)
DSP122117119(Pam)
NCAR124986502
OCU100352005(PAM)
OPI101526566(PAM)
TUP102499925(PAM)
CFA479145(PAM)
VVP112915565(PAM)
VLG121489468(PAM)
AML100484534(PAM)
UMR103656467(PAM)
UAH113255028(PAM)
UAR123799268(PAM)
ELK111148403
LLV125101073
MPUF101671790(PAM)
ORO101383156(PAM)
EJU114208638(PAM)
ZCA113929120(PAM)
MLX118017056(PAM)
FCA101084598(PAM)
PYU121012392(PAM)
PBG122491636(PAM)
PTG102961161(PAM)
PPAD109267636(PAM)
AJU106982276(PAM)
HHV120220005(PAM)
BTA280890(PAM)
BOM102271872(PAM)
BIU109562372(PAM)
BBUB102409727(PAM)
CHX102190130(PAM)
OAS101112815(PAM)
ODA120863478(PAM)
CCAD122439492(PAM)
SSC100526040(PAM)
CFR102509591(PAM)
CBAI105082012(PAM)
CDK105103083(PAM)
VPC102529765(PAM)
BACU103008694(PAM)
LVE103088789(PAM)
OOR101274063(PAM)
DLE111183960(PAM)
PCAD102993897(PAM)
PSIU116750498(PAM)
ECB791244(PAM)
EPZ103555847(PAM)
EAI106831159(PAM)
MYB102257709(PAM)
MYD102752613(PAM)
MMYO118655718(PAM)
MLF102422620(PAM)
MNA107544178(PAM)
PKL118703757(PAM)
HAI109394174(PAM)
DRO112307140(PAM)
SHON118977247(PAM)
AJM119047249(PAM)
PDIC114494537(PAM)
PHAS123818032(PAM)
MMF118641919(PAM)
RFQ117024680(PAM)
PALE102894575(PAM)
PGIG120590776(PAM)
PVP105304427(PAM)
RAY107509145(PAM)
MJV108391703(PAM)
TOD119260954(PAM)
SARA101547265(PAM)
LAV100655604(PAM)
TMU101356870
DNM101428897(PAM)
MDO100030601(PAM)
GAS123236274(PAM)
SHR100929728(PAM)
PCW110199219(PAM)
OAA100073355(PAM)
GGA427274(PAM)
PCOC116229802(PAM)
CJO107306340(PAM)
NMEL110389678(PAM)
APLA101795983(PAM)
ACYG106043740(PAM)
AFUL116500419(PAM)
TGU100227923(PAM)
LSR110477851(PAM)
SCAN103822855(PAM)
PMOA120500582(PAM)
OTC121332561(PAM)
PRUF121355586(PAM)
GFR102039677(PAM)
FAB101821831(PAM)
PHI102114573(PAM)
PMAJ107215969(PAM)
CCAE111940620(PAM)
CCW104693194(PAM)
ETL114064047(PAM)
ZAB102069666(PAM)
FPG101920860(PAM)
FCH102052743(PAM)
CLV102087217(PAM)
EGZ104135057(PAM)
NNI104010298(PAM)
ACUN113489698(PAM)
TALA104363524(PAM)
PADL103920863(PAM)
ACHC115336613(PAM)
AROW112970164(PAM)
NPD112951384(PAM)
DNE112988498 112992418
ASN102374229(PAM)
AMJ102559599(PAM)
CPOO109308144(PAM)
GGN109297455(PAM)
PSS102462977(PAM)
CMY102946187(PAM)
CPIC101942761(PAM)
TST117879396(PAM)
CABI116815270(PAM)
MRV120407700(PAM)
ACS100562563(pam)
PVT110079386(PAM)
SUND121924102(PAM)
PBI103055156(PAM)
TSR106548589(PAM)
PGUT117674609(PAM)
VKO123031660(PAM)
PMUA114606841(PAM)
ZVI118076918(PAM)
GJA107121208(PAM)
STOW125436547(PAM)
XLA379207(pam.L) 397736(pam.S)
XTR100170159(pam)
NPR108797815(PAM)
RTEM120931440(PAM)
BBUF120992549(PAM)
BGAR122924652(PAM)
DRE570822(pam)
SRX107715844 107737006
SANH107670040 107702561
SGH107558261(pam) 107560403
CCAR109097266 109098036
CAUA113053993 113109552
PPRM120483160(pam)
MAMB125255806(pam)
IPU108277198(pam)
PHYP113543505(pam)
SMEO124393835(pam)
TFD113639276(pam)
AMEX103031431(pam)
EEE113576732(pam)
TRU101062613(pam)
TNGGSTEN00013653G001
LCO104938829(pam)
CGOB115017065(pam)
ELY117269835(pam)
PLEP121960283(pam)
SLUC116041373(pam)
ECRA117958843(pam)
PFLV114570620(pam)
GAT120831508(pam)
PPUG119226240(pam)
MSAM119914308(pam)
CUD121525000(pam)
MZE101484633(pam)
ONL100700800(pam)
OAU116319154(pam)
OLA101164528(pam)
OML112140341(pam)
XMA102227462(pam)
XCO114149523(pam)
XHE116724732(pam)
PRET103473165(pam)
PFOR103152322
PLAI106947015(pam)
PMEI106922489(pam)
GAF122819675(pam)
CVG107098487(pam)
CTUL119797739(pam)
GMU124872307(pam)
NFU107395057(pam)
KMR108246466(pam)
ALIM106522199(pam)
NWH119424389(pam)
AOCE111579145(pam)
CSEM103389193(pam)
POV109637635(pam)
SSEN122758574(pam)
HHIP117771409(pam)
LCF108877750(pam)
SDU111221118(pam)
SLAL111659622(pam)
XGL120806189(pam)
HCQ109530660(pam)
BPEC110161642(pam)
MALB109960744(pam)
SASA106571984(pam)
OTW112219988(pam)
OMY110523161(pam)
OGO123989512(pam)
ONE115118014(pam)
SALP111961960(pam)
SNH120025478(pam)
ELS105020460(pam)
SFM108929922(pam)
PKI111835769(pam)
AANG118212765(pam)
LOC102682623(pam)
PSPA121302893(pam) 121315078
ARUT117409376 117963343
LCM102348819(PAM)
CMK103178402(pam)
RTP109919477(pam)
BFO118407264 118407715 118409685 118410160
BBEL109469541 109470824 109482227
CIN100186640 100186964
SCLV120333720 120334207
SPU579753 587198
APLC110987818
SKO102803906 102808073
DMEDmel_CG3832(Phm)
DER6548056
DSE6615827
DSIDsimw501_GD24986(Dsim_GD24986)
DYADyak_GE11501
DAN6494903
DSR110191555
DPODpse_GA17718
DPE6591044
DMN108160696 117191325
DWI6637882
DGR6560041
DMODmoj_GI20691
DAZ108616319
DNV115564826
DHE111600106
DVI6625978
CCAT101458361
BOD118682072
MDE101895308
SCAC106088463
LCQ111678022
AGAAgaP_AGAP007420
ACOZ120952059
AARA120897302
AAG5570501
AALB109413127
CQUCpipJ_CPIJ000277
CPII120427083
CNS116350394
AME412898
ACER108000884
ALAB122720000
BIM100742180
BBIF117216931
BVK117231991
BVAN117157478
BTER100644842
BPYO122567009
CCAL108626394
OBB114872670
MGEN117226599
NMEA116432582
CGIG122395525
SOC105198561
MPHA105834205
AEC105152181
ACEP105625891
PBAR105431355
VEM105559346
HST105188766
DQU106747041
CFO105248300
FEX115245145
LHU105677788
PGC109858237
OBO105277440
PCF106786055
PFUC122525337
VPS122633116
CSOL105366100
TPRE106653747
MDL103573620
CGLO123270423
FAS105268001
DAM107035829
AGIF122852438
CCIN107270765
TCA664519
DPA109533856
SOY115876829
ATD109600562
CSET123322259
AGB108907353
LDC111506322
NVL108560955
APLN108737569
PPYR116165581
OTU111425349
BMOR101742277
BMAN114244909
MSEX115441270
DPLKGM_201498
BANY112055870 112056221
PMAC106716851
PPOT106111965
PXU106124068
PRAP110993134
ZCE119829691
HAW110383814
TNL113496548
SLIU111353259
OFU114363928
PXY105388351
API100161384
DNX107173105
AGS114129500 114129504
RMD113552161
BTAB109039943
DCI103511470
CLEC106666670
HHAL106684730 112211536
NLU111058068
PHUPhum_PHUM593160
FOC113217583
ZNE110835112
CSEC111863563
FCD110845847 110845914
DPXDAPPUDRAFT_307337 DAPPUDRAFT_330720
DMK116925123 116930770 123466817
PVM113815933 113815942 113827570
PJA122255319 122266205
PCHN125025825
HAME121866941 121871701
PCLA123757522 123765107
PTRU123506128 123519064
HAZT108671591 108671767
EAF111695161 111695463 111695791 111696841 111716718
LSM121115245 121121168 121122000 121129607
DSV119442465 119442579
RSAN119385941 119387394
RMP119159392 119159463
VDE111254545
VJA111264503
TUT107368260
DPTE113791349 113796289
DFR124492876 124494306
CSCU111617460 111638043
PTEP107445310
SDM118185578 118185580 118205964
CELCELE_T19B4.1(pamn-1) CELE_Y71G12B.4(pghm-1)
CBRCBG_14919(Cbr-pamn-1) CBG_22199(Cbr-pghm-1)
LOALOAG_02126
NAINECAME_00981
HROHELRODRAFT_90150
LGILOTGIDRAFT_128636 LOTGIDRAFT_157833
PCAN112553876
BGT106051779 106070207 106074305
GAE121377754 121383843 121386141
HRF124135743 124135744 124146994 124147038
HRJ124255774 124255836 124288942
CRG105320938
MYI110443164
PMAX117333861 117334163 117335171
MMER123522828 123565313
OBI106870427
OSN115218053 115220401
LAK106162187
SMMSmp_156530
SHXMS3_0014254
OVIT265_08837
EGLEGR_00446
NVE116601431 5505959 5513959
EPA110253509 110253517
ATEN116290559 116306504
ADF107333635
AMIL114961864 114967143
PDAM113668474 113672672
SPIS111322235 111331755
DGT114522559 114541151
XEN124452262 124454721
HMG100212200 100212498
TADTRIADDRAFT_63754
AQU100636212
CRECHLRE_03g152850v5
VCNVOLCADRAFT_120843
CSLCOCSUDRAFT_65252
CVRCHLNCDRAFT_34137
APROF751_4456
OLUOSTLU_15206(PAM1)
OTAOT_ostta04g04860
BPGBathy08g04470
MPPMICPUCDRAFT_60313
 » 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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