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Literature summary extracted from
- Investigation of calcium-dependent activity and conformational dynamics of zebra fish 12-lipoxygenase (2017), Biochim. Biophys. Acta, 1861, 2099-2111 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.11.31 | recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 | Danio rerio |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.11.31 | additional information | construction of a soluble version of zf12-LOX by mutagenesis. Mutation of the putative calcium-responsive amino acids in N-PLAT domain of soluble zf12-LOX and analysis of the oligomeric state, stability, structural integrity and conformational changes of zf12-LOX in response to calcium. Soluble zf12-LOX and the N-PLAT domain-mutant both proteins exist as compact monomers in solution, and the enzyme activity of soluble zf12-LOX is significantly increased in presence of calcium, the stimulatory effect of calcium on zf12-LOX is related to a change in protein structure. In contrast, enzyme with a mutated calcium regulatory site has reduced activity-response to calcium and restricted large re-modeling, suggesting that it retains a closedstate in response to calcium. Ca2+-dependent regulation is associated with different domain conformation(s) that might change the accessibility to substrate-binding site in response to calcium | Danio rerio |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.13.11.31 | additional information | - |
additional information | Michaelis-Menten kinetics | Danio rerio |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.31 | Ca2+ | the specific activity of recombinant soluble zf12-LOX mutant is increased by nearly 75% (25 nmol/min/mg) in the presence of calcium as compared to that in its absence (7 nmol/min/mg), while for the site-2 mutant, it is 5 nmol/min/mg irrespective of the presence of calcium. Ca2+ decreases the aggregation temperature of soluble zf12-LOX mutant, while secondary structure is maintained. Presence of Ca2+ induces increase in molecular dimensions of soluble zf12-LOX mutant | Danio rerio |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.31 | arachidonate + O2 | Danio rerio | - |
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.31 | Danio rerio | Q7T2A9 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.11.31 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography | Danio rerio |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.31 | arachidonate + O2 | - |
Danio rerio | (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate | - |
? | |
| 1.13.11.31 | linoleate + O2 | - |
Danio rerio | (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate | - |
? | |
| 1.13.11.31 | additional information | structure-function analysis | Danio rerio | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.13.11.31 | monomer | 1 * 75000, recombinant His-tagged enzyme, SDS-PAGE | Danio rerio |
| 1.13.11.31 | More | structure-function analysis | Danio rerio |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.31 | 12-lipoxygenase | - |
Danio rerio |
| 1.13.11.31 | ALOX12 | - |
Danio rerio |
| 1.13.11.31 | zf12-LOX | - |
Danio rerio |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.31 | 22 | - |
assay at | Danio rerio |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.31 | 7.5 | - |
assay at | Danio rerio |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.31 | additional information | structure-function analysis | Danio rerio |
| 1.13.11.31 | physiological function | the enzyme is required for normal embryonic development in the fish | Danio rerio |
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