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

This is an abbreviated version!
For detailed information about 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), go to the full flat file.

Word Map on EC 1.2.4.4

Reaction

3-methyl-2-oxobutanoate
+
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
=
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine
 +
CO2
 + 2 H+

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)

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D108N
-
less thermostable than wild type enzyme
D200A
-
less thermostable than wild type enzyme
D200A/D108N
-
the mutant is defective in folding and assembly and as no detectable overall activity
D200N
-
less thermostable than wild type enzyme
D295A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased activity compared to the wild-type
E198Q/D200N
-
the mutant is defective in folding and assembly and as no detectable overall activity
F364C
-
E1alpha-missense mutation in type IA maple syrup urine disease that causes the occurence of exclusively alpha,beta dimers
H146A
-
site-directed mutagenesis, mutation of a beta'-subunit residue, no reductive acylation activity, low decarboxylation activity
H147N
-
site-directed mutagenesis, mutation of a beta'-subunit residue, no reductive acylation activity, low decarboxylation activity
H291A
-
site-directed mutagenesis, mutation of a alpha-subunit residue, highly reduced activity compared to the wild-type E1b component
H291N
-
site-directed mutagenesis, mutation of a alpha-subunit residue, highly reduced activity compared to the wild-type E1b component
H291Q
-
site-directed mutagenesis, mutation of a alpha-subunit residue, highly reduced activity compared to the wild-type E1b component
R287A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, highly increased Km and reduced activity compared to the wild-type
R301A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased Km and reduced activity compared to the wild-type
S292D
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, reduced activity compared to the wild-type E1b component
S292E
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, highly reduced activity compared to the wild-type E1b component
S292N
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, reduced activity compared to the wild-type E1b component
S292Q
S302A
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, increased activity compared to the wild-type E1b component
T265R
-
missense mutation in type IA maple syrup urine disease that causes the occurence of both alpha2beta2 tetramers and lower molecular weight species
Y300A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased Km and reduced activity compared to the wild-type
Y300F
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased Km and reduced activity compared to the wild-type
Y368C
-
missense mutation in type IA maple syrup urine disease that causes the occurence of both alpha2beta2 tetramers and lower molecular weight species
Y393N
-
E1alpha-missense mutation in type IA maple syrup urine disease that causes the occurence of exclusively alpha,beta dimers
S313A
-
twofold increase in Km-value but no change in turnover-number
S315A
-
mutation has no effect on Km-value or turnover-number
S319A
-
mutation has no effect on Km-value or turnover-number
D296A
-
inactive enzyme, no ability of component E1 apoenzyme to reconstitute with thiamine diphosphate
H292A
-
inactive enzyme, no binding of thiamine diphosphate
R288A
-
inactive enzyme, no detectable phosphorylation
S293A
S293E
S293E/S303E
-
mutation in the alpha-subunit, no activity
S303A
-
mutation in the alpha-subunit, no effect upon enzyme activity
S303E
-
mutation in the alpha-subunit, no effect upon enzyme activity
additional information