Application | Comment | Organism |
---|---|---|
analysis | enzymatic oxidation of L-lactate catalyzed by flavocytochrome b2 and coupled with formazan production from nitrotetrazolium blue can be used for L-lactate assay in food samples. A high correlation between results of the proposed method and reference ones proves the possibility to use flavocytochrome b2-catalysed reaction for enzymatic measurement of L-lactate in biotechnology and food chemistry | Ogataea angusta |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Ogataea angusta | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + 2 ferricytochrome c | Ogataea angusta | - |
pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 ferricytochrome c | Ogataea angusta tr1 | - |
pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 flavocytochrome b2 | Ogataea angusta | - |
pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 flavocytochrome b2 | Ogataea angusta tr1 | - |
pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ogataea angusta | W1QKE8 | - |
- |
Ogataea angusta tr1 | W1QKE8 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme by anion exchange chromatography | Ogataea angusta |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
11 | - |
crude enzyme, cell-free extracts, pH 7.8, 20°C | Ogataea angusta |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + 2 ferricytochrome c | - |
Ogataea angusta | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 ferricytochrome c | - |
Ogataea angusta tr1 | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 flavocytochrome b2 | - |
Ogataea angusta | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
(S)-lactate + 2 flavocytochrome b2 | - |
Ogataea angusta tr1 | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? | |
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 | Ogataea angusta | ? | - |
? | |
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 | Ogataea angusta tr1 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | the enzyme is a tetramer with four identical subunits, each consisting of FMN- and heme-binding domains | Ogataea angusta |
Synonyms | Comment | Organism |
---|---|---|
FC b2 | - |
Ogataea angusta |
flavocytochrome b2 | - |
Ogataea angusta |
L-lactate-cytochrome c oxidoreductase | - |
Ogataea angusta |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Ogataea angusta |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Ogataea angusta |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ferricytochrome c | - |
Ogataea angusta | |
flavocytochrome b2 | - |
Ogataea angusta | |
FMN | each of the four subunits contains a flavin mononucleotide prosthetic group | Ogataea angusta | |
heme | each of the four subunits contains a beta-type heme | Ogataea angusta |
General Information | Comment | Organism |
---|---|---|
physiological function | L-lactate-cytochrome b oxidoreductase catalyses the electron transfer from L-lactate to cytochrome b in yeast mitochondria | Ogataea angusta |