1.14.11.1: gamma-butyrobetaine dioxygenase
This is an abbreviated version!
For detailed information about gamma-butyrobetaine dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.1
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1.14.11.1
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cardioprotective
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carnitine-dependent
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3-2,2,2-trimethylhydrazinium
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mildronate
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trimethyllysine
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mid1
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alpha4
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medicine
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d-carnitine
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dihydrate
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drug development
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molecular biology
- 1.14.11.1
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cardioprotective
-
carnitine-dependent
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3-2,2,2-trimethylhydrazinium
- mildronate
- trimethyllysine
- mid1
-
alpha4
- medicine
- d-carnitine
- dihydrate
- drug development
- molecular biology
Reaction
Synonyms
4-trimethylaminobutyric acid dioxygenase, alpha-butyrobetaine hydroxylase, BBD, BBH, BBOX, BBOX1, Bu hydroxylase, butyrobetaine hydroxylase, gamma butyrobetaine hydroxylase, gamma-BBD, gamma-BBH, gamma-buryrobetaine dioxygenase, gamma-butyrobetaine dioxygenase, gamma-butyrobetaine hydroxylase, gamma-butyrobetaine hydroxylase 1, GBB hydroxylase, GBBH, hBBOX, oxygenase, gamma-butyrobetaine di-, psBBOX
ECTree
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General Information
General Information on EC 1.14.11.1 - gamma-butyrobetaine dioxygenase
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drug target
inhibitors of gamma-butyrobetaine hydroxylase 1 (BBOX1) could be a potential therapeutic option for Triple-negative breast cancer
evolution
metabolism
physiological function
additional information
the GBBH residues involved in zinc binding are evolutionary conserved in all sequenced eukaryotes more complex than Caenorhabditis elegans
evolution
comparison of properties, substrate specificities, and structures of the human enzyme (PDB ID 3O2G) and the enzyme from Pseudomonas sp. AK1, detailed overview
evolution
comparison of properties, substrate specificities, and structures of the human enzyme (PDB ID 3O2G) and the enzyme from Pseudomonas sp. AK1, detailed overview
evolution
the enzyme belongs to the 2-oxoglutarate/Fe(II) dependent oxygenase family
evolution
the enzyme belongs to the 2-oxoglutarate/Fe(II) dependent oxygenase family
evolution
the enzyme belongs to the superfamily of Fe(II) and 2OG dependent dioxygenases
evolution
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the enzyme belongs to the 2-oxoglutarate/Fe(II) dependent oxygenase family
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evolution
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comparison of properties, substrate specificities, and structures of the human enzyme (PDB ID 3O2G) and the enzyme from Pseudomonas sp. AK1, detailed overview
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gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step in the biosynthesis of carnitine i.e. the stereoselective hydroxylation of gamma-butyrobetaine (GBB)
metabolism
gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step in the biosynthesis of carnitine i.e. the stereoselective hydroxylation of gamma-butyrobetaine (GBB)
metabolism
gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step of carnitine biosynthesis
metabolism
the enzyme catalyses the second, essential step of carnitine biosynthesis
metabolism
last limiting enzyme of the L-carnitine biosynthesis pathway and plays an important role in catalyzing the hydroxylation of gamma-butyrobetaine to L-carnitine
metabolism
the enzyme catalyzes the final step in the biosynthesis of L-carnitine in humans
metabolism
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gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step in the biosynthesis of carnitine i.e. the stereoselective hydroxylation of gamma-butyrobetaine (GBB)
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biosynthesis of carnitine, important role in beta-oxidation of fatty acid
physiological function
GBBH is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine. L-Carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy
physiological function
enzyme BBOX catalyses the stereospecific C-3 hydroxylation of gamma-butyrobetaine (GBB) to give L-carnitine
physiological function
gamma-butyrobetaine hydroxylase (BBOX) catalyzes the conversion of gamma butyrobetaine (GBB) to L-carnitine, which is involved in the generation of metabolic energy from long-chain fatty acids
physiological function
gamma-butyrobetaine hydroxylase (BBOX) is a 2-oxoglutarate-dependent oxygenase that catalyses the stereoselective C-3 hydroxylation of gamma-butyrobetaine to give L-carnitine. L-Carnitine is involved in fatty acid metabolism
physiological function
gamma-butyrobetaine hydroxylase (BBOX) is a nonheme Fe(II)- and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of gamma-butyrobetaine in the final step of carnitine biosynthesis
physiological function
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gamma-butyrobetaine hydroxylase (BBOX) is a nonheme Fe(II)- and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of gamma-butyrobetaine in the final step of carnitine biosynthesis
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homology structure modeling with bound Ni2+ and N-oxalglycine, modeled based on human BBOX structure, DB ID 2O2G
additional information
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homology structure modeling with bound Ni2+ and N-oxalglycine, modeled based on human BBOX structure, DB ID 2O2G
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