KEGG   ENZYME: 1.1.3.2
Entry
EC 1.1.3.2                  Enzyme                                 

Name
L-lactate oxidase;
lctO (gene name);
LOX
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
Sysname
(S)-lactate:oxygen 2-oxidoreductase
Reaction(IUBMB)
(S)-lactate + O2 = pyruvate + H2O2 [RN:R11996]
Reaction(KEGG)
R11996
Substrate
(S)-lactate [CPD:C00186];
O2 [CPD:C00007]
Product
pyruvate [CPD:C00022];
H2O2 [CPD:C00027]
Comment
Contains flavin mononucleotide (FMN). The best characterized enzyme is that from the bacterium Aerococcus viridans. The enzyme is widely used in biosensors to measure the lactate concentration in blood and other tissues.
History
EC 1.1.3.2 created 1961, transferred 1972 to EC 1.13.12.4, reinstated 2018
Orthology
K10530  L-lactate oxidase
Genes
ECP: ECP_3788
ECI: UTI89_C4909
EAB: ECABU_c48710
ELU: UM146_21760
STY: STY1444
STT: t1529
SEX: STBHUCCB_16270
SENT: TY21A_07760
STM: STM1620
SEO: STM14_1959
SENI: CY43_08270
SPT: SPA1249
SEK: SSPA1158
SEI: SPC_2115
SEC: SCH_1616(gox)
SHB: SU5_02232
SED: SeD_A1722
SENE: IA1_08025
SBG: SBG_1447
SBZ: A464_1656
PLU: plu4371
PAY: PAU_03922
PMR: PMI3575
PHAU: PH4a_09260
PSI: S70_10120
PSX: DR96_1174
PAET: NCTC13378_00696(lldD)
KAI: K32_03900(lox)
LLA: L78730(lctO)
LLK: LLKF_1317(lctO)
LLT: CVCAS_1218(lctO)
LLS: lilo_1190(lctO)
LLX: NCDO2118_1281(lctO)
LLJ: LG36_1149(lctO)
LLW: kw2_1200(lctO)
LGR: LCGT_0940
LGV: LCGL_0961
SPY: SPy_0414(lctO)
SPZ: M5005_Spy0340(lctO)
SPYM: M1GAS476_0407(lctO)
SPYA: A20_0391(lctO)
SPG: SpyM3_0297(lctO)
SPS: SPs1560
SPH: MGAS10270_Spy0339(lctO)
SPI: MGAS10750_Spy0338(lctO)
SPJ: MGAS2096_Spy0360(lctO)
SPK: MGAS9429_Spy0343(lctO)
SPF: SpyM51519(lctO)
SPB: M28_Spy0328(lctO)
STG: MGAS15252_0366(lctO)
STX: MGAS1882_0366(lctO)
SOZ: Spy49_0335(lctO)
STZ: SPYALAB49_000371(lctO)
SPYH: L897_01860
SPN: SP_0715(lctO-2)
SPD: SPD_0621(lctO)
SPR: spr0627(lctO)
SPW: SPCG_0663(lctO)
SJJ: SPJ_0655(lctO)
SNV: SPNINV200_06300(lctO)
SPX: SPG_0648
SNT: SPT_0731(lctO)
SND: MYY_0751
SPNN: T308_03345
SNE: SPN23F06390(lctO)
SNC: HMPREF0837_10999(lctO)
SNM: SP70585_0761(lctO)
SPP: SPP_0725(lctO)
SNI: INV104_05940(lctO)
SPNG: HMPREF1038_00731(lctO)
SNB: SP670_0763(lctO)
SNP: SPAP_0691
SNX: SPNOXC06470(lctO)
SNU: SPNA45_01046(lctO)
SPNE: SPN034156_16960(lctO)
SPNU: SPN034183_06480(lctO)
SPNM: SPN994038_06370(lctO)
SPNO: SPN994039_06380(lctO)
SDS: SDEG_0467
SDA: GGS_0455(lctO)
SDC: SDSE_0485(lctO)
SMB: smi_1435(lctO)
SOR: SOR_1410(lctO)
SANC: SANR_1809(lctO)
SANS: DK43_01600
SIK: K710_1519
STRN: SNAG_1378
SPEI: EHW89_07810(lctO)
SGW: D7D53_01845(lctO)
SPLR: C0J00_07810(lctO)
SLAT: J4854_08570(lctO)
LJO: LJ_1826
LJF: FI9785_1781(lox)
LJH: LJP_1765c
LGA: LGAS_1864
LCR: LCRIS_01388(lctO)
LAM: LA2_10015
LPW: LpgJCM5343_17890(lldD)
LCA: LSEI_2339
LCW: BN194_07870(GLO5) BN194_24790(haox)
LCB: LCABL_07830(loxL) LCABL_25240(loxL)
LRH: LGG_00707(lctO) LGG_02356(lctO)
LRL: LC705_00676(lctO) LC705_02348(lctO)
LPL: lp_3586(lox)
LPJ: JDM1_2867(lox)
LPT: zj316_0187(lox)
LPS: LPST_C2930(lox)
LPZ: Lp16_2802
LBH: Lbuc_0007
LBN: LBUCD034_0007(lctO)
PPE: PEPE_0922
PPEN: T256_04505
LSA: LCA_1399(loxL2)
WCE: WS08_0532
WCT: WS74_0533
EHR: EHR_08130
ECAS: ECBG_02725
EMU: EMQU_2062
EDU: LIU_11425
ESG: EsVE80_24370(lctO)
THL: TEH_25400(lctO)
CRN: CAR_c06050(loxL) CAR_c11800(haox)
CARC: NY10_1308
CARN: FPV25_03910(lctO)
JDA: BW727_101663(hmo)
AIN: Acin_0614
EBM: SG0102_17560(lctO)
SIJ: SCIP_1210
MYR: MYRA21_0969(lldD)
MPW: MPR_3501
 » show all
Reference
1  [PMID:2818595]
  Authors
Duncan JD, Wallis JO, Azari MR
  Title
Purification and properties of Aerococcus viridans lactate oxidase.
  Journal
Biochem Biophys Res Commun 164:919-26 (1989)
DOI:10.1016/0006-291X(89)91546-5
Reference
2  [PMID:8589073]
  Authors
Maeda-Yorita K, Aki K, Sagai H, Misaki H, Massey V
  Title
L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a common structural theme.
  Journal
Biochimie 77:631-42 (1995)
DOI:10.1016/0300-9084(96)88178-8
  Sequence
Reference
3  [PMID:10508058]
  Authors
Gibello A, Collins MD, Dominguez L, Fernandez-Garayzabal JF, Richardson PT
  Title
Cloning and analysis of the L-lactate utilization genes from Streptococcus iniae.
  Journal
Appl Environ Microbiol 65:4346-50 (1999)
DOI:10.1128/AEM.65.10.4346-4350.1999
  Sequence
[sik:K710_1519]
Reference
4  [PMID:17007814]
  Authors
Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, Morimoto Y
  Title
The crystal structure of L-lactate oxidase from Aerococcus viridans at 2.1A resolution reveals the mechanism of strict substrate recognition.
  Journal
Biochem Biophys Res Commun 350:249-56 (2006)
DOI:10.1016/j.bbrc.2006.09.025
  Sequence
Reference
5  [PMID:18367206]
  Authors
Furuichi M, Suzuki N, Dhakshnamoorhty B, Minagawa H, Yamagishi R, Watanabe Y, Goto Y, Kaneko H, Yoshida Y, Yagi H, Waga I, Kumar PK, Mizuno H
  Title
X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism.
  Journal
J Mol Biol 378:436-46 (2008)
DOI:10.1016/j.jmb.2008.02.062
  Sequence
Reference
6  [PMID:27302031]
  Authors
Stoisser T, Brunsteiner M, Wilson DK, Nidetzky B
  Title
Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr(215) in Aerococcus viridans lactate oxidase.
  Journal
Sci Rep 6:27892 (2016)
DOI:10.1038/srep27892
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.3.2
IUBMB Enzyme Nomenclature: 1.1.3.2
ExPASy - ENZYME nomenclature database: 1.1.3.2
BRENDA, the Enzyme Database: 1.1.3.2

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