Any feedback?
Literature summary for 1.13.11.34 extracted from
- Identification and characterization of a new protein isoform of human 5-lipoxygenase (2016), PLoS ONE, 11, e0166591 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Homo sapiens |  |
| additional information | the enzyme mutant 5-LODELTA4 stimulates wild-type 5-LO activity and product formation at low protein concentrations | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ALOX5, located on chromosome 10q11.21, it spans a region of 71.9 kbp and consists of 13 introns named A-M and 14 exons, semiquantitative PCR enzyme expression analysis. Recombinant expression of enzyme mutant 5-LODELTA4 in HEK-293T cells from expression plasmid, recombinant expression of soluble 5-LODELTA4 mutant and of wild-type enzyme 5-LO in Escherichia coli strain BL21(DE3) | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | identification of a protein isoform of human 5-LO that lacks exon 4, termed 5-LODELTA4, identified in cells of lymphoid origin, namely the Burkitt lymphoma cell lines Raji and BL41 as well as primary B and T cells, semiquantitative PCR enzyme expression analysis. Deletion of exon 4 does not shift the reading frame and therefore the mRNA is not subjected to non-mediated mRNA decay. Enzyme mutant 5-LODELTA4 isoform is a stable protein in eukaryotic cells. The isoform itself lacks canonical enzymatic activity as it misses the non-heme iron but it still retains ATP-binding affinity. Whilst the catalytic domain of wild-type 5-LO is destabilized by calcium, addition of calcium has no influence on the catalytic domain of 5-LODELTA4. The enzyme mutant 5-LODELTA4 stimulates wild-type 5-LO activity and product formation at low protein concentrations | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | whilst the catalytic domain of wild-type 5-LO is destabilized by calcium, addition of calcium has no influence on the catalytic domain of 5-LODELTA4 | Homo sapiens | |
| Fe2+ | a non-heme iron that is required for catalytic activity | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arachidonate + O2 | Homo sapiens | - |
(5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P09917 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant soluble 5-LODELTA4 mutant and wild-type enzyme 5-LO from Escherichia coli strain BL21(DE3) by ATP affinity chromatography and anion exchange chromatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| B-lymphocyte | - |
Homo sapiens | - |
| BL-41 cell | - |
Homo sapiens | - |
| Burkitt lymphoma cell | - |
Homo sapiens | - |
| dendritic cell | - |
Homo sapiens | - |
| leukocyte | - |
Homo sapiens | - |
| macrophage | - |
Homo sapiens | - |
| mast cell | - |
Homo sapiens | - |
| monocyte | - |
Homo sapiens | - |
| additional information | 5-LO is mainly expressed in polymorphonuclear leukocytes, monocytes/macrophages, dendritic cells, mast cells and B cells | Homo sapiens | - |
| RAJI cell | - |
Homo sapiens | - |
| T-lymphocyte | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arachidonate + O2 | - |
Homo sapiens | (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 77900, SDS-PAGE | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5-lipoxygenase | - |
Homo sapiens |
| 5-LO | - |
Homo sapiens |
| ALOX5 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | a protein isoform of human 5-LO that lacks exon 4, termed 5-LODELTA4, lacks canonical enzymatic activity as it misses the non-heme iron but it still retains ATP-binding affinity. The enzyme mutant 5-LODELTA4 stimulates wild-type 5-LO activity and product formation at low protein concentrations | Homo sapiens |
| physiological function | leukotrienes are inflammatory mediators that play a pivotal role in many diseases like asthma bronchiale, atherosclerosis and in various types of cancer. The key enzyme for generation of leukotrienes is the 5-lipoxygenase, 5-LO, that catalyzes the initial steps in the conversion of arachidonate to the instable epoxide leukotriene A4 (LTA4) via the intermediate 5(S)-hydroperoxy-6,8,11,14-(E,Z,Z,Z)-eicosatetraenoic acid (5-HpETE). LTA4 can then be metabolized by the LTA4 hydrolase to the potent chemoattractant and leukocyte activator LTB4 or conjugated with glutathione to the cysteinyl leukotriene LTC4 by LTC4 synthase | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
