1.3.8.7: medium-chain acyl-CoA dehydrogenase

This is an abbreviated version!
For detailed information about medium-chain acyl-CoA dehydrogenase, go to the full flat file.

Word Map on EC 1.3.8.7

Reaction

a medium-chain acyl-CoA
+
electron-transfer flavoprotein
=
a medium-chain trans-2,3-dehydroacyl-CoA
+
reduced electron-transfer flavoprotein

Synonyms

ACAD-9, ACADM, ACD, acyl CoA dehydrogenase, acyl coenzyme A dehydrogenase, acyl dehydrogenase, acyl-CoA dehydrogenase, acyl-CoA dehydrogenase-9, dehydrogenase, acyl coenzyme A, EC 1.3.2.2, FadE, fatty acyl coenzyme A dehydrogenase, fatty-acyl-CoA dehydrogenase, general ACAD, general acyl CoA dehydrogenase, LCAD, LipB, MCAD, MCADH, medium chain acyl-CoA dehydrogenase, medium chain-specific acyl-CoA oxidase, medium-chain acyl CoA dehydrogenase, medium-chain acyl-CoA dehydrogenase, medium-chain acyl-coenzyme A dehydrogenase, medium-chain coenzyme A dehydrogenase, pMCAD, PP_1893, PP_2039, PP_2048, PP_2437

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.8 With a flavin as acceptor
                1.3.8.7 medium-chain acyl-CoA dehydrogenase

Engineering

Engineering on EC 1.3.8.7 - medium-chain acyl-CoA dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A1010C
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
A151T
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
A293E
-
less than 5% residual octanoyl-CoA oxidation activity
A52V
-
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
A533C
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
A985G
D221N
-
less than 5% residual octanoyl-CoA oxidation activity
D266G
-
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
D320Y
-
less than 5% residual octanoyl-CoA oxidation activity
D79X
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
delT125, E126
-
less than 5% residual octanoyl-CoA oxidation activity
E376G
-
the rate of dehydrogenation is lowered by approximately 5 orders of magnitude
E376Q
E376Q/E99G
-
the rate of dehydrogenation is lowered by 4-5 orders of magnitude
F194S
-
less than 5% residual octanoyl-CoA oxidation activity
G127A
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, not clearly associated with a clinical phenotype
G170R
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
G242R
-
less than 5% residual octanoyl-CoA oxidation activity
G285R
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
G799A
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
I208T
-
about 5% residual octanoyl-CoA oxidation activity
K153T
-
less than 5% residual octanoyl-CoA oxidation activity
K276X
-
less than 5% residual octanoyl-CoA oxidation activity
K304E
K329E
L59F
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
L73DELTA
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
M303V
-
less than 5% residual octanoyl-CoA oxidation activity
N169D
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
N354K
-
about 8% residual octanoyl-CoA oxidation activity
N396Y
-
involved in MCAD deficiency with a MCAD activity of 11.2% compared to the wild type enzyme, in combination with the deletion mutation DELTA449-CTGA-452
P128X
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
Q20R
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R123K
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R206C
-
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
R256S
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R334K
-
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
R413S
-
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
R6H
-
about 45% residual octanoyl-CoA oxidation activity
T1229G
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
T168A
-
thermostability is markedly decreased, 80% lowered activity in ferricinum assay
T199C
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, not clearly associated with a clinical phenotype
T255E
-
same activity with octanoyl-CoA as wild-type, activity/chain length profile is, however, narrower
T255E/E376G
-
chimeric medium-long chain acyl-CoA dehydrogenase, has 20% of the activity of medium-chain acyl-CoA dehydrogenase and 25% that of long-chain acyl-CoA dehydrogenase activity with its best substrates octanoyl-CoA and dodecanoyl-CoA respectively, activity maximum is shifted to C12 and C14-CoA, enzyme shows an enhanced rate of reoxidation with oxygen
T255E/E376T
-
shifts the chain length activity profile to higher values, drastic reduction of maximal velocity
T92T
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
T96I
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
V247A
-
less than 5% residual octanoyl-CoA oxidation activity
V362V
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
Y158H
-
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
Y312S
-
about 8% residual octanoyl-CoA oxidation activity
Y394X
-
less than 5% residual octanoyl-CoA oxidation activity
Y67H
-
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
K304E
-
maximal velocity of the mutant protein is only one third of the wild-type value. 16% higher activity with the natural electron acceptor, electron transferring flavoprotein, than the wild-type enzyme. Decreased stability at temperatures above 42C compared to wild-type enzyme
R256K
-
3.6fold increase in Km-value for octanoyl-CoA, 45fold decrease in turnovernumber with octanoyl-CoA compared to wild-type enzyme
Y375A
-
very low acyl-CoA dehydrogenase activity
Y375E
-
inactive
Y375F
-
very low acyl-CoA dehydrogenase activity
Y375K
-
very low acyl-CoA dehydrogenase activity, mutant exhibits acyl-CoA oxidase activity
Y42H
-
mutant enzyme has approximately the same maximal velocity as the wild-type enzyme, the KM-value for octanoyl-CoA is 1.6fold higher than the wild-type value. 7% higher activity with the natural electron acceptor, electron transferring flavoprotein, than the wild-type enzyme. Decreased stability at temperatures above 42C compared to wild-type enzyme
E276Q
-
no detectable activity in ferricenium assay
E376P
-
no detectable activity in ferricenium assay
additional information