KEGG   ENZYME: 1.1.3.29
Entry
EC 1.1.3.29                 Enzyme                                 
Name
N-acylhexosamine oxidase;
N-acyl-D-hexosamine oxidase;
N-acyl-beta-D-hexosamine:oxygen 1-oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
Sysname
N-acyl-D-hexosamine:oxygen 1-oxidoreductase
Reaction(IUBMB)
(1) N-acetyl-D-glucosamine + O2 + H2O = N-acetyl-D-glucosaminate + H2O2 (overall reaction) [RN:R01203];
(1a) N-acetyl-D-glucosamine + O2 = N-acetyl-D-glucosamino-1,5-lactone + H2O2 [RN:R12973];
(1b) N-acetyl-D-glucosamino-1,5-lactone + H2O = N-acetyl-D-glucosaminate (spontaneous) [RN:R12974];
(2) N-acetyl-D-galactosamine + O2 + H2O = N-acetyl-D-galacotsaminate + H2O2 (overall reaction) [RN:R12975];
(2a) N-acetyl-D-galactosamine + O2 = N-acetyl-D-galactosamino-1,5-lactone + H2O2 [RN:R12976];
(2b) N-acetyl-D-galactosamino-1,5-lactone + H2O = N-acetyl-D-galactosaminate (spontaneous) [RN:R12977]
Reaction(KEGG)
Substrate
N-acetyl-D-glucosamine [CPD:C00140];
O2 [CPD:C00007];
H2O [CPD:C00001];
N-acetyl-D-glucosamino-1,5-lactone [CPD:C22488];
N-acetyl-D-galactosamine [CPD:C01132];
N-acetyl-D-galactosamino-1,5-lactone [CPD:C22489]
Product
N-acetyl-D-glucosaminate [CPD:C01133];
H2O2 [CPD:C00027];
N-acetyl-D-glucosamino-1,5-lactone [CPD:C22488];
N-acetyl-D-galacotsaminate;
N-acetyl-D-galactosamino-1,5-lactone [CPD:C22489];
N-acetyl-D-galactosaminate [CPD:C03408]
Comment
The enzyme, found in bacteria, also acts more slowly on N-acetyl-D-mannosamine.
History
EC 1.1.3.29 created 1992, modified 2022
Orthology
K26080  N-acylhexosamine oxidase
Genes
KLEAO703_02750
YPEYPO0308
YPKy0566
YPHYPC_0697
YPAYPA_3976
YPNYPN_3361
YPMYP_0464(glcD1)
YPPYPDSF_3664
YPGYpAngola_A0676
YPZYPZ3_0265
YPTA1122_03600
YPDYPD4_0270
YPXYPD8_0271
YPWCH59_1556
YPJCH55_3455
YPVBZ15_3264
YPLCH46_606
YPSYPTB0364
YPOBZ17_2206
YPIYpsIP31758_3776
YPYYPK_3866
YPBYPTS_0387
YPQDJ40_2045
YPUBZ21_3734
YPRBZ20_1748
YPCBZ23_4004
YPFBZ19_3835
YSIBF17_09925
DYEEO087_03910
PFLPFL_0338
PPRCPFLCHA0_c03430
PFCPflA506_0033
PFBVO64_3080
PTVAA957_14265
PVRPverR02_00205
POIBOP93_00170
PRXHRH33_01065
PSOSPOS17_0335
PANRA7J50_1605
PSEPC4K39_0350
PTRTHU722_0001180
PSAMHU731_016245
PPEGKUA23_00170
CRZD1345_00310
CHAECH06BL_00600
AMAHDLM_1403
RSORSc0050
RSCRCFBP_21395
RSLRPSI07_3328
RSNRSPO_c03310
RSMCMR15_30852
RSEF504_57
RSYRSUY_31940
RPIRpic_3700
RPFRpic12D_3377
RMNTK49_03295
RINACS15_3846
RPUCDC45_00260
RSGJK151_02115
RWEKOL96_24230
BMABMA2895
BMVBMASAVP1_A3473
BMLBMA10229_A1646
BMNBMA10247_3077
BMALDM55_933
BMAEDM78_788
BMAQDM76_910
BMAIDM57_1647
BMAFDM51_2511
BMAZBM44_282
BMABBM45_3006
BPSBPSL3339
BPMBURPS1710b_0113(glcD1)
BPLBURPS1106A_3978
BPDBURPS668_3897
BPRGBP346_A4084
BPSEBDL_2035
BPSMBBQ_3495
BPSUBBN_81
BPSDBBX_427
BPZBP1026B_I3577
BPQBPC006_I4016
BPKBBK_1524
BPSHDR55_1162
BPSABBU_2201
BPSOX996_774
BUTX994_2793
BTEBTH_I3218
BTQBTQ_3158
BTJBTJ_2537
BTZBTL_452
BTDBTI_226
BTVBTHA_542
BTHEBTN_909
BTHMBTRA_656
BTHADR62_1102
BTHLBG87_665
BOKDM82_3036
BOCBG90_1680
BUUWS70_00895
BSAVWS86_01315
BHGI6G56_19655
BULBW21_309
BUDAQ610_00950
AXONH44784_043681
AXNAX27061_2534
AXXERS451415_02524
ADTAPT56_12480
ASWCVS48_23045
ACHRC2U31_18540
ACHBDVB37_17430
VPEVarpa_1307
CPRACPter91_0977
ACMAciX9_3805
GMAAciX8_3480 AciX8_4014
GRWFTO74_07490
TSAAciPR4_1704 AciPR4_2445
TRSTerro_2944
TALBFTW19_05120
EDAGWR55_05100 GWR55_06340 GWR55_12210
EDGH7846_10845 H7846_11285
ADINH7849_15695
 » show all
Reference
1
  Authors
Horiuchi, T.
  Title
Purification and properties of N-acyl-D-hexosamine oxidase from Pseudomonas sp. 15-1.
  Journal
Agric Biol Chem 53:361-368 (1989)
Reference
2  [PMID:34709726]
  Authors
Rembeza E, Boverio A, Fraaije MW, Engqvist MKM.
  Title
Discovery of Two Novel Oxidases Using a High-Throughput Activity Screen.
  Journal
Chembiochem 23:e202100510 (2022)
DOI:10.1002/cbic.202100510
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.3.29
IUBMB Enzyme Nomenclature: 1.1.3.29
ExPASy - ENZYME nomenclature database: 1.1.3.29
BRENDA, the Enzyme Database: 1.1.3.29
CAS: 121479-58-1
LinkDB

DBGET integrated database retrieval system