1.2.1.25: branched-chain alpha-keto acid dehydrogenase system
This is an abbreviated version!
For detailed information about branched-chain alpha-keto acid dehydrogenase system, go to the full flat file.
Word Map on EC 1.2.1.25
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1.2.1.25
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maple
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syrup
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pdha1
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dihydrolipoamide
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alpha2beta2
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transacylase
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keto-acids
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bckdhb
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dihydrolipoyl
- 1.2.1.25
-
maple
- syrup
- pdha1
- dihydrolipoamide
-
alpha2beta2
-
transacylase
-
keto-acids
- bckdhb
-
dihydrolipoyl
Reaction
Synonyms
2-oxoisovalerate dehydrogenase, alpha-ketoisovalerate dehydrogenase, BCKD, BCKD complex, BCKDalpha, BCKDbeta, BCKDC, BCKDH, BCKDHA, BCKDHB, bkdA, BKDH, branched chain alpha-keto acid dehydrogenase complex, branched chain keto-acid dehydrogenase, branched-chain alpha-keto acid dehydrogenase complex, branched-chain alpha-ketoacid dehydrogenase, branched-chain alpha-ketoacid dehydrogenase complex, branched-chain alpha-ketoacid dehydrogenase complex E1alpha subunit, branched-chain ketoacid dehydrogenase, branched-chain-keto-acid dehydrogenase alpha, branched-chain-keto-acid dehydrogenase beta, dehydrogenase, 2-oxoisovalerate (acylating), E1alpha subunit, E1beta subunit, mitochondrial branched-chain keto-acid dehydrogenase, More
ECTree
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Reference on EC 1.2.1.25 - branched-chain alpha-keto acid dehydrogenase system
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Namba, Y.; Yoshizawa, K.; Ejima, A.; Hayashi, T.; Kaneda, T.
Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched chain alpha-keto acid dehydrogenase. I. Purification and properties of the enzyme from Bacillus subtilis
J. Biol. Chem.
244
4437-4447
1969
Bacillus subtilis
Ganesan, B.; Dobrowolski, P.; Weimer, B.C.
Identification of the leucine-to-2-methylbutyric acid catabolic pathway of Lactococcus lactis
Appl. Environ. Microbiol.
72
4264-4273
2006
Lactococcus lactis, Lactococcus lactis IL1403
Adeva-Andany, M.; Lopez-Maside, L.; Donapetry-Garcia, C.; Fernanndez-Fernanndez, C.; Sixto-Leal, C.
Enzymes involved in branched-chain amino acid metabolism in humans
Amino Acids
49
1005-1028
2017
Homo sapiens (P12694 AND P21953)
Blair, M.; Neinast, M.; Arany, Z.
Whole-body metabolic fate of branched-chain amino acids
Biochem. J.
478
765-776
2021
Homo sapiens (P12694 AND P21953), Rattus norvegicus (P12694 AND P21953), Mus musculus (P50136 AND Q6P3A8)
Bunik, V.; Brand, M.
Generation of superoxide and hydrogen peroxide by side reactions of mitochondrial 2-oxoacid dehydrogenase complexes in isolation and in cells
Biol. Chem.
399
407-420
2018
Bos taurus, Homo sapiens (P12694 AND P21953), Mus musculus, Saccharomyces cerevisiae
Cui, Q.; Zhou, F.; Liu, W.; Tao, Y.
Avermectin biosynthesis stable functional expression of branched chain alpha-keto acid dehydrogenase complex from Streptomyces avermitilis in Escherichia coli by selectively regulating individual subunit gene expression
Biotechnol. Lett.
39
1567-1574
2017
Streptomyces avermitilis (Q53592)
Xing, G.; Ren, M.; Verma, A.
Divergent induction of branched-chain aminotransferases and phosphorylation of branched chain keto-acid dehydrogenase is a potential mechanism coupling branched-chain keto-acid-mediated-astrocyte activation to branched-chain amino acid depletion-mediated cognitive deficit after traumatic brain injury
J. Neurotrauma
35
2482-2494
2018
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Hull, J.; Usmari Moraes, M.; Brookes, E.; Love, S.; Conway, M.
Distribution of the branched-chain alpha-ketoacid dehydrogenase complex E1alpha subunit and glutamate dehydrogenase in the human brain and their role in neuro-metabolism
Neurochem. Int.
112
49-58
2018
Homo sapiens (P12694 AND P21953)
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