KEGG   ENZYME: 1.1.3.17
Entry
EC 1.1.3.17                 Enzyme                                 
Name
choline oxidase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
Sysname
choline:oxygen 1-oxidoreductase
Reaction(IUBMB)
choline + 2 O2 + H2O = betaine + 2 H2O2 (overall reaction) [RN:R08212];
(1a) choline + O2 = betaine aldehyde + H2O2 [RN:R01022];
(1b) betaine aldehyde + O2 + H2O = betaine + H2O2 [RN:R08211]
Reaction(KEGG)
Substrate
choline [CPD:C00114];
O2 [CPD:C00007];
H2O [CPD:C00001];
betaine aldehyde [CPD:C00576]
Product
betaine [CPD:C00719];
H2O2 [CPD:C00027];
betaine aldehyde [CPD:C00576]
Comment
A flavoprotein (FAD). In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [6]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in those plants, animals and bacteria that use two separate enzymes.
History
EC 1.1.3.17 created 1978, modified 2005, modified 2007
Pathway
ec00260  Glycine, serine and threonine metabolism
ec01100  Metabolic pathways
Orthology
K17755  choline oxidase
Genes
MMCMmcs_2464
MKMMkms_2509
MJLMjls_2501
MDXBTO20_10210
MGROFZ046_21730
MSPGF6B93_06805
MRFMJO55_15765
MGIMflv_3085
MSPMspyr1_24000
MCBMycch_3082
MVQMYVA_3361
MAUUNCTC10437_03326(betA_3)
MMAGMMAD_49040
MTYMTOK_49630
MPSCMPSYJ_32570
MARZMARA_06160
MAUBMAUB_20700
MMUCC1S78_022320
MMATMMAGJ_51060
MSEIMSEDJ_45610
CVACVAR_1534(betA1)
CHNA605_05285
CTERA606_06065
CCGCCASEI_03545
CGYCGLY_08220(betA1)
CAMGCAMM_03220
CPRECsp1_13250(codA_2)
CYZC3B44_02525
CLIAC3E79_10435
NCYNOCYR_3120(codA)
NBRO3I_018420
NSLBOX37_17140
NSRNS506_02934
NTPCRH09_09050
NOZDMB37_02125
NODFOH10_13640
NAHF5544_24845
NYALTV02_18365
RHARHA1_ro01805 RHA1_ro01877
ROPROP_14830 ROP_15550
ROAPd630_LPD05964 Pd630_LPD06042
RHBNY08_1329
RFAA3L23_04564(codA)
RHSA3Q41_03707(codA)
RHWBFN03_11820
RTMG4H71_19750
RKOJWS14_09255 JWS14_09600
GPOGPOL_c02820
GORKTR9_0772
GOQACH46_04295
GTABCM27_04215
GRUGCWB2_03940(codA)
GOMD7316_02647(codA_2)
GAVC5O27_01100
GODGKZ92_03690
GJIH1R19_03635
GOILK459_08520
GHNMVF96_04005
GAMIIHQ52_06545
TPRTpau_2794
TSMASU32_15640
TPULTPB0596_16740
SRTSrot_2479
DTMBJL86_2075
TOYFO059_06125
SMASAVERM_6946
SGRSGR_1535
SGBWQO_27655
SCBSCAB_76051
SVLStrvi_2803
SHYSHJG_2834
SHOSHJGH_2598
SRCM271_11505
SMALSMALA_6294
SSOII1A49_35300
SFISFUL_5923
STREGZL_02072
SLDT261_1293
SLCSL103_14845 SL103_24015
SCZABE83_06570
SRWTUE45_01815(codA_1)
SCLFBB341_00200
SGMGCM10017557_69170
SCADDN051_31670
SNRSNOUR_09290(codA)
SNWBBN63_33030
SAUOBV401_35430
SGVB1H19_33965
STROSTRMOE7_04980 STRMOE7_31465
SLKSLUN_36120
SDXC4B68_34525
STIRDDW44_01370
SFICEIZ62_31670
SGALCP966_05405
SSPODDQ41_09845
SFYGFH48_33530
SCAVCVT27_27195
SPHVF9278_06485
SPLACP981_31980
SHUNDWB77_00888(codA_1) DWB77_06707(codA_2)
SCYGS1361_07790(codA1)
SDWK7C20_30570
SAUHSU9_029035
SPEUCGZ69_03610
SXNIAG42_07525
SANUK7396_06610
STRYEQG64_28425
SINEKI385_05940 KI385_36285
SLFJEQ17_38775
SDECL3078_08055
KABB7C62_29330
CMICMM_1950
CMHVO01_09045
LEBG7066_05325
MANTBHD05_14485
ARTArth_3743
ARRARUE_c04830
ARWMB46_09520
ARZAUT26_03710
ARQBWQ92_22440
ARNCGK93_02610
ARXARZXY2_3153
ACRYAC20117_09005
ARTHC3B78_18505
ASUNKG104_15950
ASUFMNQ99_17080
AAUAAur_0512
PUEFV140_03985
PNVJMY29_02345
ACHAchl_3494 Achl_3687
PSULAU252_11510
PSNINIBR502771_06600
AAIAARI_07270(codA)
GARAOZ07_04060
GCRGcLGCM259_0568(codA)
GLUF0M17_03745
GMINMP99_04270
GMYXH9_05025
KRHKRH_18100(betA)
KPLKPaMU14_03130
KFVAS188_03705
KRSEQG70_13465
KVRCIB50_0001287(codA)
MYUM8233_07735
RTERIDM49_10670
RKRI6G21_06285
NAEBHE16_09330
AULDCC27_000810
PAEYKUF55_03675
BFABfae_22540
BRXBH708_07565
BRVCFK39_03640
BGGCFK41_05355
BRZCFK38_07585
BRRC1N80_07690
BKIM4486_12825
LMOIVV02_21505
BLYA2T55_10975
BLINBLSMQ_2409
BLUTEW640_10735
BCAUI6G59_14555
SENSACE_5373
SACGFDZ84_22600
AOIAORI_2600(betA)
AJAAJAP_25825(codA)
AMYCCU254_10935
AMYBBKN51_05615
AABA4R43_14000
AMYYYIM_31165(codA)
AORISD37_14070
PSEEFRP1_06385
PSEHXF36_16415
PSEQAD006_14005
PECQAD017_21830
PHHAFB00_02425
PAUTPdca_46070
PBROHOP40_33570
SACEGIY23_14910
AEYCDG81_08830
RXYRxyl_0758
 » show all
Reference
1  [PMID:599154]
  Authors
Ikuta S, Imamura S, Misaki H, Horiuti Y.
  Title
Purification and characterization of choline oxidase from Arthrobacter globiformis.
  Journal
J Biochem (Tokyo) 82:1741-9 (1977)
DOI:10.1093/oxfordjournals.jbchem.a131872
Reference
2  [PMID:1987142]
  Authors
Rozwadowski KL, Khachatourians GG, Selvaraj G.
  Title
Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli.
  Journal
J Bacteriol 173:472-8 (1991)
DOI:10.1128/JB.173.2.472-478.1991
Reference
3  [PMID:12795615]
  Authors
Rand T, Halkier T, Hansen OC
  Title
Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis.
  Journal
Biochemistry 42:7188-94 (2003)
DOI:10.1021/bi0274266
Reference
4  [PMID:15369826]
  Authors
Gadda G, Powell NL, Menon P.
  Title
The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase.
  Journal
Arch Biochem Biophys 430:264-73 (2004)
DOI:10.1016/j.abb.2004.07.011
Reference
5  [PMID:15713082]
  Authors
Fan F, Gadda G.
  Title
On the catalytic mechanism of choline oxidase.
  Journal
J Am Chem Soc 127:2067-74 (2005)
DOI:10.1021/ja044541q
Reference
6  [PMID:12466265]
  Authors
Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T, Takabe T
  Title
Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica.
  Journal
J Biol Chem 278:4932-42 (2003)
DOI:10.1074/jbc.M210970200
Reference
7  [PMID:14678796]
  Authors
Fan F, Ghanem M, Gadda G
  Title
Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance.
  Journal
Arch Biochem Biophys 421:149-58 (2004)
DOI:10.1016/j.abb.2003.10.003
  Sequence
Reference
8  [PMID:12637017]
  Authors
Gadda G.
  Title
Kinetic mechanism of choline oxidase from Arthrobacter globiformis.
  Journal
Biochim Biophys Acta 1646:112-8 (2003)
DOI:10.1016/S1570-9639(03)00003-7
Other DBs
ExplorEnz - The Enzyme Database: 1.1.3.17
IUBMB Enzyme Nomenclature: 1.1.3.17
ExPASy - ENZYME nomenclature database: 1.1.3.17
BRENDA, the Enzyme Database: 1.1.3.17
CAS: 9028-67-5

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