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2.3.1.61: dihydrolipoyllysine-residue succinyltransferase

This is an abbreviated version!
For detailed information about dihydrolipoyllysine-residue succinyltransferase, go to the full flat file.

Word Map on EC 2.3.1.61

Reaction

succinyl-CoA
+
enzyme N6-(dihydrolipoyl)lysine
=
CoA
 +
enzyme N6-(S-succinyldihydrolipoyl)lysine

Synonyms

AceF, dihydrolipoamide acyltransacetylase, dihydrolipoamide S-succinyltransferase, dihydrolipoamide succinyltransferase, dihydrolipoic transsuccinylase, dihydrolipolyl succinyltransferase, dihydrolipolyl transsuccinylase, dihydrolipoyl succinyl transferase, dihydrolipoyl succinyltransferase, dihydrolipoyl transsuccinylase, DLST, DSCD, E2 component of alpha-ketoglutarate dehydrogenase complex, E2 subcomponent of the alpha-ketoglutarate dehydrogenase complex, E2o, KGD2, lipoate succinyltransferase, lipoic transsuccinylase, lipoyl transsuccinylase, OGDC-E2, SucB, succinyl-CoA:dihydrolipoate S-succinyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.61 dihydrolipoyllysine-residue succinyltransferase

Engineering

Engineering on EC 2.3.1.61 - dihydrolipoyllysine-residue succinyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D374A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 2.1% compared to the wild type enzyme
D374N
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.7% compared to the wild type enzyme
D379A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.5% compared to the wild type enzyme
H375A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 2fold compared to the wild type enzyme
H375C
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 1% compared to the wild type enzyme
H375G
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 5fold compared to the wild type enzyme
H375N
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 0.5% compared to the wild type enzyme
H375W
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 54fold compared to the wild type enzyme
R376A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 56% compared to the wild type enzyme
T323A
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 45% compared to the wild type enzyme
T323S
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 43% compared to the wild type enzyme
D423A
D423DEL
-
the mutant shows reduced activity compared to the wild type enzyme
D423E
D423G
D423S
H419A
-
the mutant shows reduced activity compared to the wild type enzyme
H419D
-
the mutant shows reduced activity compared to the wild type enzyme
H419del
H419G
-
the mutant shows reduced activity compared to the wild type enzyme
H419S
D423A
-
site-directed mutagenesis, the corresponding Km value of the D423A variant is 233% of the wild-type enzyme Km, while the kcat value of the variant is 4% compared to the wild-type enzyme
-
D423E
-
site-directed mutagenesis, the corresponding activity of the D423E variant is 30% of the wild-type activity
-
D423G
-
site-directed mutagenesis, the corresponding Km value of the D423S variant is 200% of the wild-type enzyme Km
-
D423S
-
site-directed mutagenesis, the corresponding Km value of the D423S variant is 161% of the wild-type enzyme Km, while the kcat value of the variant is 9% compared to the wild-type enzyme
-
H419S
-
site-directed mutagenesis, the mutant shows a the kcat value of 6% compared to the wild-type
-
D423A
-
the mutant shows reduced activity compared to the wild type enzyme
-
D423E
-
the mutant shows reduced activity compared to the wild type enzyme
-
D423G
-
the mutant shows reduced activity compared to the wild type enzyme
-
D423S
-
the mutant shows reduced activity compared to the wild type enzyme
-
H419S
-
the mutant shows reduced activity compared to the wild type enzyme
-
additional information
-
generation of enzyme knockout mutants, the zebrafish mutant schneckentempo, phenotype ste, exhibits bradycardia. The ste mutation is a guanine to adenine nucleotide transition in the splice donor site of intron 5 of the zdlst gene, ENSDARG00000014230