BRENDA - Enzyme Database
show all sequences of 1.14.18.7

Functional association of cell death suppressor, Arabidopsis Bax inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b5

Nagano, M.; Ihara-Ohori, Y.; Imai, H.; Inada, N.; Fujimoto, M.; Tsutsumi, N.; Uchimiya, H.; Kawai-Yamada, M.; Plant J. 58, 122-134 (2009)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
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Saccharomyces cerevisiae
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Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome b5
Arabidopsis thaliana FAH1 and FAH2 have no Cb5-like domain, and interact with electron transfer protein Cb5. Bax inhibitor-1 is a widely conserved cytoprotective protein localized in the endoplasmic reticulum membrane and also interacts with Cb5. Arabidopsis thaliana Bax inhibitor-1 -mediated suppression of cell death in yeast requires Saccharomyces cerevisiae fatty acid hydroxylase 1, which has a Cb5-like domain at the N terminus and interacts with Bax inhibitor-1
Arabidopsis thaliana
cytochrome b5
fatty acid hydroxylase 1 has a Cb5-like domain at the N terminus and interacts with plant cryoprotective protein Bax inhibitor-1
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome b5
Arabidopsis thaliana FAH1 and FAH2 have no Cb5-like domain, and interact with electron transfer protein Cb5. Bax inhibitor-1 is a widely conserved cytoprotective protein localized in the endoplasmic reticulum membrane and also interacts with Cb5. Arabidopsis thaliana Bax inhibitor-1 -mediated suppression of cell death in yeast requires Saccharomyces cerevisiae fatty acid hydroxylase 1, which has a Cb5-like domain at the N terminus and interacts with Bax inhibitor-1
Arabidopsis thaliana
cytochrome b5
fatty acid hydroxylase 1 has a Cb5-like domain at the N terminus and interacts with plant cryoprotective protein Bax inhibitor-1
Saccharomyces cerevisiae
General Information
General Information
Commentary
Organism
physiological function
Arabidopsis thaliana Bax inhibitor-1 -mediated suppression of cell death in yeast requires Saccharomyces cerevisiae fatty acid hydroxylase 1, which has a Cb5-like domain at the N terminus and interacts with Bax inhibitor-1
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
physiological function
Arabidopsis thaliana Bax inhibitor-1 -mediated suppression of cell death in yeast requires Saccharomyces cerevisiae fatty acid hydroxylase 1, which has a Cb5-like domain at the N terminus and interacts with Bax inhibitor-1
Saccharomyces cerevisiae
Other publictions for EC 1.14.18.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746153
Nagano
Arabidopsis Bax inhibitor-1 p ...
Saccharomyces cerevisiae
Planta
240
77-89
2014
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734960
Nagano
Arabidopsis sphingolipid fatty ...
Arabidopsis thaliana
Plant Physiol.
159
1138-1148
2012
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734909
Nagano
Functional association of cell ...
Arabidopsis thaliana, Saccharomyces cerevisiae
Plant J.
58
122-134
2009
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734124
Mitchell
Fah1p, a Saccharomyces cerevis ...
Arabidopsis thaliana
J. Biol. Chem.
272
28281-28288
1997
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