Entry
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
BRITE hierarchy
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)
Substrate
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
CCAN : 109689129(Pam) 109698017
XLA : 379207(pam.L) 397736(pam.S)
SANH : 107670040 107702561
SGH : 107558261(pam) 107560403
CCAR : 109097266 109098036
CAUA : 113053993 113109552
CGIB : 127966314 128021433
MASI : 127432330 127433275
PSPA : 121302893(pam) 121315078
ARUT : 117409376 117963343
PMRN : 116950708 116954932
BFO : 118407264 118407715 118409685 118410160
BBEL : 109469541 109470824 109482227
SCLV : 120333720 120334207
LPIC : 129261786 129261787 129261976
ARUN : 117295427 117296047
DSI : Dsimw501_GD24986(Dsim_GD24986)
AALB : 109413127 109418106
CFEL : 113376829 113378460
MQU : 128996417 128996418 128996419
DPX : DAPPUDRAFT_307337 DAPPUDRAFT_330720
DMK : 116925123 116930770 123466817
PVM : 113815933 113815942 113827570
PMOO : 119577060 119577876
HAME : 121866941 121871701
PCLA : 123757522 123765107
PTRU : 123506128 123519064
HAZT : 108671591 108671767
EAF : 111695161 111695463 111695791 111696841 111716718
LSM : 121115245 121121168 121122000 121129607
PPOI : 119101386 119101422 119102798 119103514
RSAN : 119385941 119387394
DPTE : 113791349 113796289
CSCU : 111617460 111638043
CVS : 136974105 136985512(Phm)
ABRU : 129955758 129972994
SDM : 118185578 118185580 118205964
LPOL : 106462234 106465021 106468167 106476744
PMEO : 129593868 129594725
CEL : CELE_T19B4.1(pamn-1) CELE_Y71G12B.4(pghm-1)
CBR : CBG_14919(Cbr-pamn-1) CBG_22199(Cbr-pghm-1)
CRQ : GCK72_001154 GCK72_001307
LGI : LOTGIDRAFT_128636 LOTGIDRAFT_157833
PVUL : 126817327 126818099 126818801
BGT : 106051779 106070207 106074305
GAE : 121377754 121383843 121386141
HRF : 124135743 124135744 124146994 124147038
HRJ : 124255774 124255836 124288942
CANU : 128175556 128175949 128177444
CVN : 111129707 111129827 111129912 111130575 111130769
PMAX : 117333861 117334163 117335171
MCAF : 127735286 127735299
MMER : 123522828 123565313
RPHI : 132728547 132759442
MAEA : 128227433 128228871 128228946
LLON : 135483204 135483295
NVE : 116601431 5505959 5513959
ATEN : 116290559 116306504
AMIL : 114961864 114967143
PDAM : 113668474 113672672
SPIS : 111322235 111331755
HSY : 130640814 130643790 130646165
» show all
Taxonomy
Reference
Authors
Bradbury AF, Finnie MD, Smyth DG.
Title
Mechanism of C-terminal amide formation by pituitary enzymes.
Journal
Reference
Authors
Glembotski CC.
Title
Further characterization of the peptidyl alpha-amidating enzyme in rat anterior pituitary secretory granules.
Journal
Reference
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
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
Reference
Authors
Murthy AS, Keutmann HT, Eipper BA.
Title
Further characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary.
Journal
Reference
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
Reference
Authors
Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM
Title
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase.
Journal
Reference
Authors
Prigge ST, Eipper BA, Mains RE, Amzel LM
Title
Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex.
Journal
Reference
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
Reference
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
Other DBs
ExPASy - ENZYME nomenclature database: 1.14.17.3
LinkDB
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