1.2.4.4: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)

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For detailed information about 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), go to the full flat file.

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Synonyms

2-oxoisocaproate dehydrogenase, 2-oxoisovalerate dehydrogenase, 2-oxoisovalerate dehydrogenase (lipoate), 2-oxoisovalerate dehydrogenase subunit alpha, alpha-keto-beta-methylvalerate dehydrogenase, alpha-ketoacid dehydrogenase, alpha-ketoisocaproate dehydrogenase, alpha-ketoisocaproic dehydrogenase, alpha-ketoisocaproic-alpha-keto-beta-methylvaleric dehydrogenase, alpha-ketoisovalerate dehydrogenase, alpha-oxoisocaproate dehydrogenase, BCDH, BCKA dehydrogenase, BCKADC, BCKD, BCKDC, BCKDH, BCKDH E1-alpha, BCKDH E1-beta, BCKDHA, BCKDHB, BCKDHc, BCOA, BCOAD, BDKG, Bkd, bkdF, branched chain alpha-ketoacid dehydrogenase complex, branched chain keto acid dehydrogenase, branched-chain (-2-oxoacid BCD) dehydrogenase, branched-chain 2-keto acid dehydrogenase, branched-chain 2-oxo acid dehydrogenase, branched-chain alpha-keto acid decarboxylase/dehydrogenase, branched-chain alpha-keto acid dehydrogenase, branched-chain alpha-keto acid dehydrogenase complex, branched-chain alpha-keto acid dehydrogenase E1beta subunit, branched-chain alpha-ketoacid dehydrogenase, branched-chain alpha-ketoacid dehydrogenase complex, branched-chain alpha-ketoacid dehydrogenase enzyme complex, branched-chain alpha-ketoacid dehydrogenase multienzyme complex, branched-chain alpha-oxo acid dehydrogenase, branched-chain keto acid dehydrogenase, branched-chain keto acid dehydrogenase complex, branched-chain ketoacid dehydrogenase, branched-chain ketoacid dehydrogenase E1, dehydrogenase, 2-oxoisocaproate, dehydrogenase, 2-oxoisovalerate (lipoate), dehydrogenase, branched chain alpha-keto acid, DHalpha, dihydrolipoyl acyl-transferase, dihydrolipoyl transacylase, E1b, E1b component, E1b component of the 2-oxo acid dehydrogenase complex, E2, EC 1.2.4.3, More

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.4 With a disulfide as acceptor

                1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)

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Results	in table
77	Activating Compound
13945	AA Sequence
9	Application
2	CAS Registry Number
25	Cloned(Commentary)
125	Cofactor
7	Crystallization (Commentary)
532	Disease/ Diagnostics
5	Expression
9	General Information
2	General Stability
48	Inhibitors
15	Ki Value [mM]
91	KM Value [mM]
27	Localization
15	Metals/Ions
40	Molecular Weight [Da]
35	Natural Substrates/ Products (Substrates)
189	Organism
5	Pathway
95	PDB ID
8	pH Optimum
2	Posttranslational Modification
44	Protein Variants
30	Purification (Commentary)
8	Reaction
5	Reaction Type
100	Reference
2	Renatured (Commentary)
93	Source Tissue
20	Specific Activity [micromol/min/mg]
7	Storage Stability
178	Substrates and Products (Substrate)
30	Subunits
129	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
2	Temperature Stability [°C]
26	Turnover Number [1/s]

Application

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Application on EC 1.2.4.4 - 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

medicine

4 entries

synthesis

Streptomyces avermitilis

-

functional expression of the branched chain alpha-keto acid dehydrogenase complex in Escherichia coli by independent and selective optimization of individual subunit genes of the complex. Codon optimization significantly improves the expression of complex component proteins BkdH and LpdA1 but expression of dehydrogenase E1 alpha subunit BkdF and dehydrogenase E1 beta subunit BkdG depends on coexpression of the BkdH gene. The optimized branched chain alpha-keto acid dehydrogenase complex supplies sufficient short branched-chain acyl-CoA to synthesize phlorisovalerophenone

762852

additional information

4 entries

medicine

Homo sapiens

-

activation of the BCKDH complex appears responsible for the increase in branched-chain amino acid catabolism caused by exercise and liver cirrhosis, branched-chain amino acid administration improves protein turnover in humans with liver cirrhosis, suggesting that branched-chain amino acid supplements are appropriate for patients with liver cirrhosis, branched-chain amino acid administration in patients with acute liver failure, especially those with high serum branched-chain amino acid concentrations, may not be appropriate because of the likelihood of branched-chain amino acid overload

675567

medicine

Rattus norvegicus

-

activation of the BCKDH complex appears responsible for the increase in branched-chain amino acid catabolism caused by exercise and liver cirrhosis, branched-chain amino acid administration improves protein turnover in rats with liver cirrhosis, suggesting that branched-chain amino acid supplements are appropriate for patients with liver cirrhosis

675567

medicine

Homo sapiens

-

variations in the gene of branched-chain alpha-keto acid dehydrogenase are associated with the occurrence of premature ovarian failure

686828

medicine

Rattus norvegicus

P11960; P35738

in male rats administered with 4 doses of 5-FU, 150 mg/kg b.wt. each, 5-FU treatment causes an increase in branched-chain alpha-keto acid dehydrogenase complex BCKDH activity that results mainly from increased dephosphorylation of the complex and is associated with an increase of phosphatase PPM1K mRNA level and reduction of BDK and dehydrogenase E1 mRNA levels

763049

additional information

Mus musculus

-

activation of the translational regulators by leucine is partly regulated by the activity of BCKDH complex

671751

additional information

Homo sapiens

-

NMR techniques to determine the structure of hbSBD and dynamics of several truncated constructs from the E2 component, including hbLBD (residues 1–84), hbSBD (residues 111–149), and a di-domain (hbDD) (residues 1–166) comprising hbLBD, hbSBD and the interdomain linker, the presence of the interdomain linker restricts the motional freedom of the hbSBD more significantly than hbLBD, the linker region likely exists as a soft rod rather than a flexible string in solution

674648

additional information

Homo sapiens

-

regulation of BCKD kinase expression by nutritional, hormonal, and pathological factors

675563

additional information

Homo sapiens

-

use of a microRNA to exert control on a metabolic pathway of amino acid catabolism

673938