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Literature summary extracted from

  • He, M.; Burghardt, T.P.; Vockley, J.
    A novel approach to the characterization of substrate specificity in short/branched chain acyl-CoA dehydrogenase (2003), J. Biol. Chem., 278, 37974-37986.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.8.5 expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.3.8.5 A383T site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 E107D/L112V/T115K/I117K site-directed mutagenesis, mutant is not stable Rattus norvegicus
1.3.8.5 F105L site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 L220M/A383T site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 L220M/L222I site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 L220M/L222I/A383T site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 L222I/A383T site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 additional information construction of deletion mutants, substrate specificity and catalytic efficiency, overview Rattus norvegicus
1.3.8.5 S177N site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 V104L site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus
1.3.8.5 V104L/F105L site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.8.5 0.0011
-
 (S)-2-methylbutanoyl-CoA mutant L222I/A383T, 32°C Rattus norvegicus
1.3.8.5 0.0015
-
 (S)-2-methylbutanoyl-CoA deletion mutant M10, 32°C Rattus norvegicus
1.3.8.5 0.002
-
 (S)-2-methylbutanoyl-CoA mutant L220M/A383T, 32°C Rattus norvegicus
1.3.8.5 0.0026
-
 (S)-2-methylbutanoyl-CoA mutant F105L, 32°C Rattus norvegicus
1.3.8.5 0.0027
-
 (S)-2-methylbutanoyl-CoA wild-type enzyme, 32°C Homo sapiens
1.3.8.5 0.0039
-
 (S)-2-methylbutanoyl-CoA wild-type enzyme, 32°C Rattus norvegicus
1.3.8.5 0.0053
-
 hexanoyl-CoA mutant L220M/A383T, 32°C Rattus norvegicus
1.3.8.5 0.0055
-
 hexanoyl-CoA mutant L222I/A383T, 32°C Rattus norvegicus
1.3.8.5 0.0107
-
 (S)-2-methylbutanoyl-CoA mutant V104L/F105L, 32°C Rattus norvegicus
1.3.8.5 0.026
-
 isobutyryl-CoA mutant L222I/A383T, 32°C Rattus norvegicus
1.3.8.5 0.035
-
 hexanoyl-CoA mutant F105L, 32°C Rattus norvegicus
1.3.8.5 0.036
-
 hexanoyl-CoA wild-type enzyme, 32°C Homo sapiens
1.3.8.5 0.044
-
 hexanoyl-CoA wild-type enzyme, 32°C Rattus norvegicus
1.3.8.5 0.049
-
 isobutyryl-CoA mutant L220M/A383T, 32°C Rattus norvegicus
1.3.8.5 0.057
-
 hexanoyl-CoA deletion mutant M10, 32°C Rattus norvegicus
1.3.8.5 0.06
-
 isobutyryl-CoA deletion mutant M10, 32°C Rattus norvegicus
1.3.8.5 0.085
-
 isobutyryl-CoA mutant V104L/F105L, 32°C Rattus norvegicus
1.3.8.5 0.095
-
 isobutyryl-CoA mutant F105L, 32°C Rattus norvegicus
1.3.8.5 0.11
-
 isobutyryl-CoA wild-type enzyme, 32°C Rattus norvegicus
1.3.8.5 0.13
-
 isobutyryl-CoA wild-type enzyme, 32°C Homo sapiens
1.3.8.5 0.15
-
 hexanoyl-CoA mutant V104L/F105L, 32°C Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.5 Homo sapiens
-
-
-
1.3.8.5 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.8.5 recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.8.5 2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+ reaction mechanism determining substrate specificity Homo sapiens
a
1.3.8.5 2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+ reaction mechanism determining substrate specificity Rattus norvegicus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.8.5 additional information
-
 activity of wild-type and mutant enzymes with different substrates, overview Rattus norvegicus
1.3.8.5 28
-
 recombinant wild-type enzyme, substrate (S)-2-methylbutanoyl-CoA Homo sapiens
1.3.8.5 35
-
 recombinant wild-type enzyme, substrate (S)-2-methylbutanoyl-CoA Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.5 (S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
-
 Homo sapiens 2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 (S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
-
 Rattus norvegicus 2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 hexanoyl-CoA + electron-transfer flavoprotein 41% of activity with (S)-2-methylbutanoyl-CoA Homo sapiens hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
-
 ?
1.3.8.5 hexanoyl-CoA + electron-transfer flavoprotein 8% of activity with (S)-2-methylbutanoyl-CoA, wild-type enzyme Rattus norvegicus hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
-
 ?
1.3.8.5 isobutyryl-CoA + electron-transfer flavoprotein 37% of activity with (S)-2-methylbutanoyl-CoA, wild-type enzyme Rattus norvegicus 2-methylacryloyl-CoA + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 isobutyryl-CoA + electron-transfer flavoprotein 6% of activity with (S)-2-methylbutanoyl-CoA Homo sapiens 2-methylacryloyl-CoA + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 additional information substrate specificity of wild-type and mutants, overview Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.8.5 More structure-function relationship, molecular modeling Homo sapiens
1.3.8.5 More structure-function relationship, molecular modeling Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
1.3.8.5 SBCAD
-
 Homo sapiens
1.3.8.5 SBCAD
-
 Rattus norvegicus
1.3.8.5 short/branched chain acyl-CoA dehydrogenase
-
 Homo sapiens
1.3.8.5 short/branched chain acyl-CoA dehydrogenase
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.8.5 32
-
 assay at Homo sapiens
1.3.8.5 32
-
 assay at Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.8.5 1200
-
 hexanoyl-CoA mutant L222I/A383T, 32°C Rattus norvegicus
1.3.8.5 1200
-
 (S)-2-methylbutanoyl-CoA mutant L222I/A383T, 32°C Rattus norvegicus
1.3.8.5 1800
-
 hexanoyl-CoA wild-type enzyme, 32°C Rattus norvegicus
1.3.8.5 2000
-
 isobutyryl-CoA deletion mutant M10, 32°C Rattus norvegicus
1.3.8.5 2000
-
 hexanoyl-CoA mutant V104L/F105L, 32°C Rattus norvegicus
1.3.8.5 2100
-
 isobutyryl-CoA mutant V104L/F105L, 32°C Rattus norvegicus
1.3.8.5 2100
-
 (S)-2-methylbutanoyl-CoA mutant V104L/F105L, 32°C Rattus norvegicus
1.3.8.5 2500
-
 hexanoyl-CoA mutant F105L, 32°C Rattus norvegicus
1.3.8.5 2600
-
 (S)-2-methylbutanoyl-CoA mutant F105L, 32°C Rattus norvegicus
1.3.8.5 2700
-
 isobutyryl-CoA mutant L220M/A383T, 32°C Rattus norvegicus
1.3.8.5 2900
-
 isobutyryl-CoA mutant F105L, 32°C Rattus norvegicus
1.3.8.5 2900
-
 isobutyryl-CoA wild-type enzyme, 32°C Homo sapiens
1.3.8.5 3000
-
 (S)-2-methylbutanoyl-CoA wild-type enzyme, 32°C Rattus norvegicus
1.3.8.5 4000
-
 (S)-2-methylbutanoyl-CoA mutant L220M/A383T, 32°C Rattus norvegicus
1.3.8.5 5100
-
 (S)-2-methylbutanoyl-CoA deletion mutant M10, 32°C Rattus norvegicus
1.3.8.5 5800
-
 hexanoyl-CoA mutant L220M/A383T, 32°C Rattus norvegicus
1.3.8.5 7400
-
 hexanoyl-CoA deletion mutant M10, 32°C Rattus norvegicus
1.3.8.5 7600
-
 hexanoyl-CoA wild-type enzyme, 32°C Homo sapiens
1.3.8.5 8100
-
 isobutyryl-CoA mutant L222I/A383T, 32°C Rattus norvegicus
1.3.8.5 8500
-
 isobutyryl-CoA wild-type enzyme, 32°C Rattus norvegicus
1.3.8.5 9700
-
 (S)-2-methylbutanoyl-CoA wild-type enzyme, 32°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.8.5 FAD
-
 Rattus norvegicus