1.3.8.4: isovaleryl-CoA dehydrogenase
This is an abbreviated version!
For detailed information about isovaleryl-CoA dehydrogenase, go to the full flat file.
Word Map on EC 1.3.8.4
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1.3.8.4
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acidemia
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acyl-coa
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inborn
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3-methylcrotonyl-coa
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isovalerylglycine
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medium-chain
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lethargy
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flavoenzyme
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isobutyryl-coa
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acylcarnitine
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isovalerylcarnitine
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flavoprotein:ubiquinone
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glutaryl-coa
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2-methylbutyryl-coa
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3-hydroxyisovaleric
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octanoyl-coa
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sweaty
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diagnostics
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medicine
- 1.3.8.4
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acidemia
- acyl-coa
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inborn
- 3-methylcrotonyl-coa
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isovalerylglycine
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medium-chain
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lethargy
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flavoenzyme
- isobutyryl-coa
- acylcarnitine
- isovalerylcarnitine
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flavoprotein:ubiquinone
- glutaryl-coa
- 2-methylbutyryl-coa
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3-hydroxyisovaleric
- octanoyl-coa
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sweaty
- diagnostics
- medicine
Reaction
Synonyms
acyl-CoA dehydrogenase, EC 1.3.99.10, i3VD, iso(3)valeryl-CoA dehydrogenase, isovaleric-CoA dehydrogenase, isovaleroyl-coenzyme A dehydrogenase, isovaleryl-coenzyme A dehydrogenase, IVD, IVDH, LiuA, Pden_3633, SBCAD, short/branched chain acyl-CoA dehydrogenase
ECTree
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Engineering
Engineering on EC 1.3.8.4 - isovaleryl-CoA dehydrogenase
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G376V
A282V
C30Y
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isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
E254G
H100R
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isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
I199M
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naturally occuring missense mutation in a Chinese infant, G39A genotype, phenotype, overview
L370M/G374A
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site-directed mutagenesis, substrate specificity similar to the wild-type enzyme, reduced activity
L95V/A99V/L103V/L370M/G374A
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site-directed mutagenesis, substitutions in the human enzyme mimick the potato isovaleryl-CoA dehydrogenase isozyme 1, which shows major 2-methylbutyryl-CoA dehydrogenase activity and rather belongs to EC 1.3.99.12, the mutant enzymes shows modified substrate specificty and also exhibits highest activity with 2-methylbutanoyl-CoA, molecular modeling of the active site
R21H
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isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
R363C
R387A
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enzyme activity detected, the mutant is less able than the mutant R387K to properly form the charge-transfer complex intermediate
R387E
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enzyme activity detected, the mutant is less able than the mutant R387K to properly form the charge-transfer complex intermediate
R387K
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enzyme activity detected, the mutant is able to form the charge-transfer complex intermediate with similar efficiency to wild-type
R387Q
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enzyme activity detected, the mutant is less able than the mutant R387K to properly form the charge-transfer complex intermediate
S97F
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isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
W13X
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naturally occuring missense mutation in a Chinese infant, C597G genotype, phenotype, overview. The mutation may destabilize the IVD monomer structure and affect the interaction between IVD and flavin adenine dinucleotide
Y166F
mutation does not block enzyme interaction with the electron transfer protein
Y371C
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isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
E246Q
E254G/G375E
site-directed mutagenesis, shows no activity with (S)-2-methylbutyryl-CoA in contrast to the wild-type enzyme, reduced activity compared to the wild-type enzyme
G375E
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
additional information
the mutation has negative effects on FAD-binding or on monomer-monomer interactions of the skunk mutant enzyme, like in strain a85, the mutant shows a odorous phenotype with prepupal lethality
G376V
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the mutation has negative effects on FAD-binding or on monomer-monomer interactions of the skunk mutant enzyme, like in strain a85, the mutant shows a odorous phenotype with prepupal lethality
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G376V
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the mutation has negative effects on FAD-binding or on monomer-monomer interactions of the skunk mutant enzyme, like in strain a85, the mutant shows a odorous phenotype with prepupal lethality
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A282V
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site-directed mutagenesis, severely affected interaction between enzyme and flavin cofactor, about 40% reduced activity compared to the wild-type enzyme
E254G
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no activity, mutant enzyme is unable to form a charge-transfer complex with substrate/product. The CD spectra indicate a perturbation of the flavin environment
R363C
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isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
site-directed mutagenesis, the recombinant IVDH enzyme mutant is obtained as an apoprotein, the protein is fully reconstituted by incubation with flavin adenine dinucleotide (FAD) at a ratio 1:20 (IVDH: FAD) molar excess. The reconstituted E246Q IVDH has no activity for isovaleryl-CoA. The mutant IVDH is unable to form charge transfer complex as a result of altering catalytic residue E246
E246Q
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site-directed mutagenesis, the recombinant IVDH enzyme mutant is obtained as an apoprotein, the protein is fully reconstituted by incubation with flavin adenine dinucleotide (FAD) at a ratio 1:20 (IVDH: FAD) molar excess. The reconstituted E246Q IVDH has no activity for isovaleryl-CoA. The mutant IVDH is unable to form charge transfer complex as a result of altering catalytic residue E246
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construction of T-DNA mutant line GK756G02, an enzyme-deficient mutant with full-length ORFs including stop codons of IVDH, phenotype, overview
additional information
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construction of T-DNA mutant line GK756G02, an enzyme-deficient mutant with full-length ORFs including stop codons of IVDH, phenotype, overview
additional information
knockout mutants atg10-1, atg5-1, and atg2-1, as well as ivdh-1 and etfqo-1 mutants, phenotypes, overview. Dark-induced increases in specific amino acid levels are compromised in atg mutants. Comparison of the amino acid levels between ivdh-1 or etfqo-1 mutants and the wild-type shows that total amino acid levels increase similarly after the dark treatment among those plants, mainly caused by increases in the BCAAs, basic amino acids, aromatic amino acids and Asn. The dark-induced increase of Glu is suppressed in ivdh-1 and etfqo-1. Among the individual amino acids that do not increase in the dark-treated wild-type, the decrease in alanine levels is exacerbated in both ivdh-1 and etfqo-1. These results show the attenuation of BCAA catabolism in the mutants. The accumulation of BCAAs after 2 days of dark treatment is enhanced in ivdh-1 and etfqo-1 compared with to wild-type supporting the suggestion that BCAAs are catabolized via IVDH and the ETF/ETFQO system from an early period of dark treatment. The ivdh-1 and etfqo-1 mutations do not affect the dark-induced increases in the levels of basic amino acids (Lys, Arg, and His) and aromatic amino acids (Phe, Tyr, and Trp) compared with to wild-type plants
additional information
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knockout mutants atg10-1, atg5-1, and atg2-1, as well as ivdh-1 and etfqo-1 mutants, phenotypes, overview. Dark-induced increases in specific amino acid levels are compromised in atg mutants. Comparison of the amino acid levels between ivdh-1 or etfqo-1 mutants and the wild-type shows that total amino acid levels increase similarly after the dark treatment among those plants, mainly caused by increases in the BCAAs, basic amino acids, aromatic amino acids and Asn. The dark-induced increase of Glu is suppressed in ivdh-1 and etfqo-1. Among the individual amino acids that do not increase in the dark-treated wild-type, the decrease in alanine levels is exacerbated in both ivdh-1 and etfqo-1. These results show the attenuation of BCAA catabolism in the mutants. The accumulation of BCAAs after 2 days of dark treatment is enhanced in ivdh-1 and etfqo-1 compared with to wild-type supporting the suggestion that BCAAs are catabolized via IVDH and the ETF/ETFQO system from an early period of dark treatment. The ivdh-1 and etfqo-1 mutations do not affect the dark-induced increases in the levels of basic amino acids (Lys, Arg, and His) and aromatic amino acids (Phe, Tyr, and Trp) compared with to wild-type plants
additional information
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construction of T-DNA mutant line GK756G02, an enzyme-deficient mutant with full-length ORFs including stop codons of IVDH, phenotype, overview
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additional information
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knockout mutants atg10-1, atg5-1, and atg2-1, as well as ivdh-1 and etfqo-1 mutants, phenotypes, overview. Dark-induced increases in specific amino acid levels are compromised in atg mutants. Comparison of the amino acid levels between ivdh-1 or etfqo-1 mutants and the wild-type shows that total amino acid levels increase similarly after the dark treatment among those plants, mainly caused by increases in the BCAAs, basic amino acids, aromatic amino acids and Asn. The dark-induced increase of Glu is suppressed in ivdh-1 and etfqo-1. Among the individual amino acids that do not increase in the dark-treated wild-type, the decrease in alanine levels is exacerbated in both ivdh-1 and etfqo-1. These results show the attenuation of BCAA catabolism in the mutants. The accumulation of BCAAs after 2 days of dark treatment is enhanced in ivdh-1 and etfqo-1 compared with to wild-type supporting the suggestion that BCAAs are catabolized via IVDH and the ETF/ETFQO system from an early period of dark treatment. The ivdh-1 and etfqo-1 mutations do not affect the dark-induced increases in the levels of basic amino acids (Lys, Arg, and His) and aromatic amino acids (Phe, Tyr, and Trp) compared with to wild-type plants
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additional information
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construction of insertion mutants, which show completely impaired growth on all acyclic terpenes tested, i.e.citronellol, geraniol, sodium salts of citronellate and geranylate, and on leucine and isovalerate, phenotype, overview