Sequence of LOX_AERVM
EC Number:1.1.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Q44467
Aerococcus viridans (strain ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC 8251 / M1)
374
40933
Reaction
Other sequences found for EC No. 1.1.3
EC Number:1.1.1.27
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
L-lactate dehydrogenase
Q44467
Aerococcus viridans (strain ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC 8251 / M1)
374
40933
Reaction
(S)-lactate + NAD+ = pyruvate + NADH + H+
Other sequences found for EC No. 1.1.1.27
EC Number:1.1.3.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
L-lactate oxidase
Q44467
Aerococcus viridans (strain ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC 8251 / M1)
374
40933
Reaction
(S)-lactate + O2 = pyruvate + H2O2
Other sequences found for EC No. 1.1.3.2
EC Number:1.13.12.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
lactate 2-monooxygenase
Q44467
Aerococcus viridans (strain ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC 8251 / M1)
374
40933
Reaction
(S)-lactate + O2 = acetate + CO2 + H2O
Other sequences found for EC No. 1.13.12.4
General information:
Sequence
0 MNNNDIEYNA PSEIKYIDVV NTYDLEEEAS KVVPHGGFNY IAGASGDEWT KRANDRAWKH
60 KLLYPRLAQD VEAPDTSTEI LGHKIKAPFI MAPIAAHGLA HTTKEAGTAR AVSEFGTIMS
120 ISAYSGATFE EISEGLNGGP RWFQIYMAKD DQQNRDILDE AKSDGATAII LTADSTVSGN
180 RDRDVKNKFV YPFGMPIVQR YLRGTAEGMS LNNIYGASKQ KISPRDIEEI AGHSGLPVFV
240 KGIQHPEDAD MAIKRGASGI WVSNHGARQL YEAPGSFDTL PAIAERVNKR VPIVFDSGVR
300 RGEHVAKALA SGADVVALGR PVLFGLALGG WQGAYSVLDY FQKDLTRVMQ LTGSQNVEDL
360 KGLDLFDNPY GYEY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1208941
Duncan J.D.,Wallis J.O.,Azari M.R.
Purification and properties of Aerococcus viridans lactate oxidase.
Biochem. Biophys. Res. Commun.
164
919-926
1989
1208942
Maeda-Yorita K.,Aki K.,Sagai H.,Misaki H.,Massey V.
L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a common structural theme.
Biochimie
77
631-642
1995
1208943
Romero M.R.,Ahumada F.,Garay F.,Baruzzi A.M.
Amperometric biosensor for direct blood lactate detection.
Anal. Chem.
82
5568-5572
2010
1208944
Hiraka K.,Kojima K.,Tsugawa W.,Asano R.,Ikebukuro K.,Sode K.
Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor.
Biosens. Bioelectron.
151
111974-111974
2020
1208945
Leiros I.,Wang E.,Rasmussen T.,Oksanen E.,Repo H.,Petersen S.B.,Heikinheimo P.,Hough E.
The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).
Acta Crystallogr. F Struct. Biol. Commun.
62
1185-1190
2006
1208946
Umena Y.,Yorita K.,Matsuoka T.,Kita A.,Fukui K.,Morimoto Y.
The crystal structure of L-lactate oxidase from Aerococcus viridans at 2.1A resolution reveals the mechanism of strict substrate recognition.
Biochem. Biophys. Res. Commun.
350
249-256
2006
1208947
Li S.J.,Umena Y.,Yorita K.,Matsuoka T.,Kita A.,Fukui K.,Morimoto Y.
Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution.
Biochem. Biophys. Res. Commun.
358
1002-1007
2007
1208948
Furuichi M.,Suzuki N.,Dhakshnamoorhty B.,Minagawa H.,Yamagishi R.,Watanabe Y.,Goto Y.,Kaneko H.,Yoshida Y.,Yagi H.,Waga I.,Kumar P.K.,Mizuno H.
X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism.
J. Mol. Biol.
378
436-446
2008
1208949
Stoisser T.,Rainer D.,Leitgeb S.,Wilson D.K.,Nidetzky B.
The Ala95-to-Gly substitution in Aerococcus viridans L-lactate oxidase revisited - structural consequences at the catalytic site and effect on reactivity with O2 and other electron acceptors.
FEBS J.
282
562-578
2015
1208950
Stoisser T.,Klimacek M.,Wilson D.K.,Nidetzky B.
Speeding up the product release: a second-sphere contribution from Tyr191 to the reactivity of L-lactate oxidase revealed in crystallographic and kinetic studies of site-directed variants.
FEBS J.
282
4130-4140
2015
1208951
Stoisser T.,Brunsteiner M.,Wilson D.K.,Nidetzky B.
Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr(215) in Aerococcus viridans lactate oxidase.
Sci. Rep.
6
27892-27892
2016
