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Information on EC 1.1.2.3 - L-lactate dehydrogenase (cytochrome)
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EC Tree
1.1.2.3 L-lactate dehydrogenase (cytochrome)IUBMB Comments
Identical with cytochrome b2; a flavohemoprotein (FMN).
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Word Map
- 1.1.2.3
- flavin
- heme
- phagocyte
-
baker
- hansenula
-
intermembrane
- anomala
- semiquinone
- ferricyanide
-
flavodehydrogenase
-
lederer
- gp91phox
- presequence
-
p40phox
-
heme-binding
-
carbanion
-
mathews
-
flavin-binding
-
chapman
- bromopyruvate
-
flavosemiquinone
- analysis
- medicine
- environmental protection
- synthesis
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
flavocytochrome b2, cytochrome b2, flavocytochrome b, fc b2, l-lactate cytochrome c oxidoreductase, l-lcr, l-lactate:cytochrome c oxidoreductase, l-lactate-cytochrome c oxidoreductase, l-lactate ferricytochrome c oxidoreductase, l-lactate:cytochrome c-oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cyb2
Cyb2A
cytochrome b2
-
-
-
-
FC b2
Fcb2
flavocytochrome b2
L(+)-lactate:cytochrome c oxidoreductase
-
-
-
-
L-lactate cytochrome c oxidoreductase
L-lactate cytochrome c reductase
-
-
-
-
L-lactate dehydrogenase [Cytochrome]
-
-
-
-
L-lactate ferricytochrome C oxidoreductase
L-lactate-cytochrome c oxidoreductase
L-lactate:cytochrom c oxidoreductase
L-lactate:cytochrome c oxidoreductase
L-lactate:cytochrome c-oxidoreductase
L-LCO
L-LCR
-
-
-
-
lactate dehydrogenase (cytochrome)
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
lactic cytochrome c reductase
-
-
-
-
flavocytochrome b2
-
-
-
-
flavocytochrome b2
-
-
L-lactate cytochrome c oxidoreductase
-
-
-
-
L-lactate ferricytochrome C oxidoreductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+
hydride transfer mechanism
-
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+
hydride transfer mechanism
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+
catalytic cycle, overview
-
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+
the hydride transfer mechanism involves the transfer of the lactate hydroxyl proton to H373 while the substrate aH atom is transferred as a hydride to the flavin mononucleotide (FMN) prosthetic group anchored in the active site
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:ferricytochrome-c 2-oxidoreductase
Identical with cytochrome b2; a flavohemoprotein (FMN).
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CAS REGISTRY NUMBER
COMMENTARY
9078-32-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-hydroxybutyrate + ferricytochrome c
2-oxobutyrate + ferrocytochrome c
-
-
-
-
?
(S)-2-hydroxyhexanoate + ferricytochrome c
2-oxohexanoate + ferrocytochrome c
-
-
-
-
?
(S)-2-hydroxyoctanoate + ferricytochrome c
2-oxooctanoate + ferrocytochrome c
-
-
-
-
?
(S)-2-hydroxyvalerate + ferricytochrome c
2-oxovalerate + ferrocytochrome c
-
-
-
-
?
(S)-lactate + 2 potassium ferricyanide
pyruvate + 2 reduced potassium ferricyanide + 2 H+
-
-
-
-
?
(S)-lactate + potassium ferricyanide
pyruvate + potassium ferrocyanide
-
-
-
-
?
(S)-phenyllactate + ferricytochrome c
phenylpyruvate + ferrocytochrome c
-
-
-
-
?
glycolate + ferricytochrome c
glyoxylate + ferrocytochrome c
-
very poor substrate
-
-
?
L-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
L-lactate + O2
? + superoxide anion
the FDH domain reacts slowly with oxygen with formation of superoxide anion when separated from its natural electron acceptor, whether isolated or included in the holoenzyme
-
-
?
phenyllactate + ferricytochrome c
phenylpyruvate + ferrocytochrome c
-
-
-
-
?
pyruvate + 2 ferrocytochrome c + 2 H+
(S)-lactate + 2 ferricytochrome c
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
absolute selectivity to L-lactate
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
Pichia kudriavzevii SD108
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
D-isomer not oxidized
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
replaces activity of EC 1.1.1.27 in limited substrate conditions
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
Rhodovulum steppense A-20s
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
r
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
r
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
D-isomer not oxidized
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
r
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
can feed electrons to respiratory chain at the level of cytochrome c
-
r
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
can feed electrons to respiratory chain at the level of cytochrome c
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
kcat/KM is 24000 fold lower with the recombinantly expressed flavocytochrome b2 flavin-binding domain compared to wild-type enzyme
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
the first step of the catalytic cycle consists of the oxidation of L-lactate by the FMN prosthetic group. FMN is later reoxidized by transferring its electrons one by one to the ferric heme. The final electron acceptor is cytochrome c
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
r
(S)-lactate + 2 flavocytochrome b2
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 flavocytochrome b2
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + 2 flavocytochrome b2
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
?
(S)-lactate + cytochrome c
pyruvate + oxidized cytochrome c
-
-
-
-
?
(S)-lactate + cytochrome c
pyruvate + oxidized cytochrome c
-
-
-
?
(S)-mandelate + ferricytochrome c
hydroxy(phenyl)acetate + ferrocytochrome c
-
-
-
-
?
(S)-mandelate + ferricytochrome c
hydroxy(phenyl)acetate + ferrocytochrome c
-
traces of activity with wild type enzyme, significant activity with A198G/L230G double mutant
-
-
?
L-lactate + ferricyanide
pyruvate + ferrocyanide + H+
-
-
-
-
?
L-lactate + ferricyanide
pyruvate + ferrocyanide + H+
-
-
-
?
L-lactate + ferricytochrome c
pyruvate + ferrocytochrome c + H+
-
-
-
-
?
L-lactate + ferricytochrome c
pyruvate + ferrocytochrome c + H+
-
-
-
?
L-lactate + ferricytochrome c
pyruvate + ferrocytochrome c + H+
-
-
-
-
?
L-lactate + ferricytochrome c
pyruvate + ferrocytochrome c + H+
flavocytochrome b2, i.e. L-lactate cytochrome c oxidoreductase, catalyzes L-lactate oxidation at the expense of cytochrome c in the mitochondrial intermembrane space in yeast and enables the latter to grow on lactate as the sole carbon source
-
-
?
L-lactate + ferricytochrome c
pyruvate + ferrocytochrome c + H+
molecular dynamics studies on active-site models of flavocytochrome b2 in complex with the substrate for analysis of the mechanism of the enzyme-catalyzed L-lactate oxidation reaction, overview. In the calculated enzyme-substrate model complex, the l-lactate alpha-OH hydrogen is hydrogen bonded to the activesite base H373 Ne, whereas the Halpha is directed towards flavin N5, suggesting that the reaction is initiated by a-OH proton abstraction
-
-
?
L-lactate + ferricytochrome c
pyruvate + ferrocytochrome c + H+
-
-
-
-
?
L-lactate + potassium ferricyanide
pyruvate + potassium ferrocyanide + H+
-
-
-
-
?
L-lactate + potassium ferricyanide
pyruvate + potassium ferrocyanide + H+
-
-
-
?
additional information
?
-
-
GOX3 shows a broad substrate spectrum, with activity toward a range of L-2-hydroxy acids. glycolate oxidase GOX3 uses L-lactate with a similar efficiency to glycolate. No activity with D-lactate
-
-
?
additional information
?
-
-
chromate-reducing ability of enzyme-overproducing recombinant cells, the highest chromate-reducing activity of the cells is achieved in the presence of 2,6-dichlorophenolindophenol
-
-
?
additional information
?
-
-
the enzyme has absolute specificity for L-lactate, yet is non-selective with respect to its electron acceptor
-
-
?
additional information
?
-
development and evaluation of an enzymatic method exploiting an enzymatic oxidation of L-lactate to pyruvate coupled with nitrotetrazolium blue (NTZB) reduction to a colored product, formazan, overview. The main advantages of the proposed method when compared to the LDH (EC 1.1.1.27)-based routine approaches are a higher sensitivity, simple procedure of analysis, usage of inexpensive, nontoxic reagents, and small amount of the enzyme. The enzyme is absolutely specific for L-lactate
-
-
?
additional information
?
-
-
development and evaluation of an enzymatic method exploiting an enzymatic oxidation of L-lactate to pyruvate coupled with nitrotetrazolium blue (NTZB) reduction to a colored product, formazan, overview. The main advantages of the proposed method when compared to the LDH (EC 1.1.1.27)-based routine approaches are a higher sensitivity, simple procedure of analysis, usage of inexpensive, nontoxic reagents, and small amount of the enzyme. The enzyme is absolutely specific for L-lactate
-
-
?
additional information
?
-
-
chromate-reducing ability of enzyme-overproducing recombinant cells, the highest chromate-reducing activity of the cells is achieved in the presence of 2,6-dichlorophenolindophenol
-
-
?
additional information
?
-
-
the enzyme has absolute specificity for L-lactate, yet is non-selective with respect to its electron acceptor
-
-
?
additional information
?
-
development and evaluation of an enzymatic method exploiting an enzymatic oxidation of L-lactate to pyruvate coupled with nitrotetrazolium blue (NTZB) reduction to a colored product, formazan, overview. The main advantages of the proposed method when compared to the LDH (EC 1.1.1.27)-based routine approaches are a higher sensitivity, simple procedure of analysis, usage of inexpensive, nontoxic reagents, and small amount of the enzyme. The enzyme is absolutely specific for L-lactate
-
-
?
additional information
?
-
-
2,6-dichlorophenolindophenol, ferricyanide and cytochrome c but not oxygen can serve as electron acceptor, rate of reduction with cytochrome c much slower than with the other possible acceptors, glycolate and L-malate do not serve as substrates
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
2,6-dichloroindophenol, ferricyanide, methylene blue, 1,2-naphthoquinone and cytochrome c can serve as electron acceptors
-
-
?
additional information
?
-
-
2,6-dichlorophenolindophenol used as electron acceptor, 10times more sensitive than ferricyanide
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
during the catalytic cycle, electrons are transferred one by one from the reduced flavin to heme b2 in the same subunit
-
-
?
additional information
?
-
the role of the flavin mononucleotide-ribityl chain 2'OH group in maintaining the conserved K349 in a geometry favoring flavin reduction, of an active site water molecule belonging to a S371-Wat-D282-H373 hydrogen-bonded chain, which modulates the reactivity of the key catalytic histidine, and of the flavin C4a-C10a locus in facilitating proton transfer from the substrate to the active-site base, favoring the initial step of the lactate dehydrogenation reaction
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
ferricyanide used as electron acceptor
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
additional information
?
-
-
electron acceptors other than ferricytochrome c used
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + 2 ferrocytochrome c + 2 H+
(S)-lactate + 2 ferricytochrome c
-
-
-
-
?
(S)-lactate + 2 ferricytochrome c
pyruvate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?