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Literature summary for 1.13.11.31 extracted from

  • Mittal, M.; Hasan, M.; Balagunaseelan, N.; Fauland, A.; Wheelock, C.; Radmark, O.; Haeggstroem, J.; Rinaldo-Matthis, A.
    Investigation of calcium-dependent activity and conformational dynamics of zebra fish 12-lipoxygenase (2017), Biochim. Biophys. Acta, 1861, 2099-2111 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Danio rerio

Protein Variants

Protein Variants Comment Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Danio rerio

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
arachidonate + O2 Danio rerio
-
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
-
?

Organism

Organism UniProt Comment Textmining
Danio rerio Q7T2A9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography Danio rerio

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arachidonate + O2
-
Danio rerio (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
-
?
linoleate + O2
-
Danio rerio (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
?
additional information structure-function analysis Danio rerio ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 75000, recombinant His-tagged enzyme, SDS-PAGE Danio rerio
More structure-function analysis Danio rerio

Synonyms

Synonyms Comment Organism
12-lipoxygenase
-
Danio rerio
ALOX12
-
Danio rerio
zf12-LOX
-
Danio rerio

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at Danio rerio

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Danio rerio

General Information

General Information Comment Organism
additional information structure-function analysis Danio rerio
physiological function the enzyme is required for normal embryonic development in the fish Danio rerio