1.13.12.4: lactate 2-monooxygenase
This is an abbreviated version!
For detailed information about lactate 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.4
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1.13.12.4
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flavin
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co2
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massey
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williams
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phlei
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flavocytochrome
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sulfite
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fmn
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smegmatis
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semiquinone
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flavoproteins
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oxalate
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reoxidation
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aerococcus
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two-electron
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pyriformis
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mandelate
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tetrahymena
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viridans
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flavoenzymes
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d-lactate
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sullivan
- 1.13.12.4
- flavin
- co2
-
massey
-
williams
- phlei
-
flavocytochrome
- sulfite
- fmn
- smegmatis
- semiquinone
- flavoproteins
- oxalate
-
reoxidation
-
aerococcus
-
two-electron
- pyriformis
- mandelate
-
tetrahymena
- viridans
-
flavoenzymes
- d-lactate
-
sullivan
Reaction
Synonyms
L-lactate monooxygenase, L-lactate-2-monooxygenase, lactate monooxygenase, lactate oxidase, lactate oxidative decarboxylase, lactate oxygenase, lactic oxidase, lactic oxygenase, LMO
ECTree
1.13.12.4 lactate 2-monooxygenaseAdvanced search results
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Engineering on EC 1.13.12.4 - lactate 2-monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G99A
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(S)-lactate binds tighter to the G99A-mutant than to wild-type
H290Q
K266M
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the rate of reduction with (S)-lactate is decreased compared with that of the wild-type enzyme, the mutant enzyme is virtually inactive
H290Q
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the ability of L-lactate to reduce the enzyme flavin is abolished, whereas reoxidation of reduced enzyme with oxygen proceeds at a rate like that found in the wild type enzyme. Unlike the situation with wild type enzyme, where the transition state analog oxalate is bound tightly in a two-step reaction involving proton uptake from solution, the mutant enzyme binds oxalate weakly, in a single step reaction. Replacing the histidine has a significant effect on the ability of the enzyme to stabilize the flavin N(5)-sulfite adduct. Sulfite is bound at least 1000fold weaker than it is in the wild type enzyme
