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2.3.1.12: dihydrolipoyllysine-residue acetyltransferase

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

Word Map on EC 2.3.1.12

Reaction

acetyl-CoA
+
enzyme N6-(dihydrolipoyl)lysine
=
CoA
 +
enzyme N6-(S-acetyldihydrolipoyl)lysine

Synonyms

acetyltransferase, lipoate, DHLTA, dihydrolipoamide acetyltransferase, dihydrolipoate acetyltransferase, dihydrolipoic transacetylase, dihydrolipoyl acetyl transferase, dihydrolipoyl acetyltransferase, dihydrolipoyl acetyltransferase component E2, dihydrolipoyl acetyltransferase E2p, dihydrolipoyl transacetylase, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial, DLAT, E2, E2p, hE2, Lat1, lipoate acetyltransferase, lipoate transacetylase, lipoic acetyltransferase, lipoic acid acetyltransferase, lipoic transacetylase, lipoylacetyltransferase, More, myelin-proteolipid O-palmitoyltransferase, palmitoyl-CoA:myelin-proteolipid O-palmitoyltransferase, pyruvate dehydrogenase complex component E2, pyruvate dehydrogenase complex component E2p, pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase component, thioltransacetylase A, transacetylase X

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.12 dihydrolipoyllysine-residue acetyltransferase

Engineering

Engineering on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K96A
-
mutation in potential lipoylation site, mutant protein entirely supports the assignment of Lys96 as the site of lipoylation
K96R
-
mutation in potential lipoylation site, mutant protein entirely supports the assignment of Lys96 as the site of lipoylation
G610C
-
500fold reduced enzymatic activity
N614D
-
9fold reduced enzymatic activity
S558A
-
200fold reduced enzymatic activity
H602C
inactive
K191E
the mutant shows 50% activity compared to the wild type enzyme
K191R
the mutant shows 79% activity compared to the wild type enzyme
K244Q
-
unlipoylatable domain
R129A
the mutant shows 34% activity compared to the wild type enzyme
R129E
the mutant shows 3.0% activity compared to the wild type enzyme
R129K
the mutant shows 77% activity compared to the wild type enzyme
R130A
the mutant shows wild type activity
R130E
the mutant shows 57% activity compared to the wild type enzyme
R150A
the mutant shows 8.0% activity compared to the wild type enzyme
R150E
the mutant shows 2.4% activity compared to the wild type enzyme
R150K
the mutant shows 5.0% activity compared to the wild type enzyme
R153E
the mutant shows 60% activity compared to the wild type enzyme
R153K
the mutant shows 83% activity compared to the wild type enzyme
R161A
the mutant shows 65% activity compared to the wild type enzyme
R161E
the mutant shows 84% activity compared to the wild type enzyme
R202E
the mutant shows 10% activity compared to the wild type enzyme
R202K
the mutant shows 86% activity compared to the wild type enzyme
K136A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
K153A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
M131A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
R135A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
R135C
-
site-directed mutagenesis, additional alkylation of the mutant enzymes with methyl, ethyl, propyl and butyl groups, the modifications cause alterations in interaction of core unit, E1 and E3 in the enzyme complex compared to the wild-type complex, thermodynamics and kinetics in comparison to the wild-type enzyme, overview
R135K
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
R135L
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
R135M
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
R139A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
R146A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
R156A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
S133A
-
site-directed mutagenesis, thermodynamics and kinetics in comparison to the wild-type enzyme
A174S
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 69%
D164A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 55%
D172A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 66%
E162A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 93%
E179A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 28%
E182A
E182Q
-
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered
E183A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 98%
F231A
-
ability to be post-translationally lipoylated remains
I176A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: not measurable
I229A
-
ability to be post-translationally lipoylated remains
I229A/F231A
-
ability to be post-translationally lipoylated remains, far-UV CD spectrum differs from wild-type enzyme
K173A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: not measurable
K276A
-
mutant shows negligible binding to human pyruvate dehydrogenase with 86fold higher KD compared to wild-type
L140A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: not measurable
L189A
-
ability to be post-translationally lipoylated remains
M194A
-
ability to be post-translationally lipoylated remains
M197A
-
ability to be post-translationally lipoylated remains
R196A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 79%
R297A
-
mutant is found to have KD 6.8fold higher than that for the wild-type, indicating a possible involvement of this residue in the interaction with human pyruvate dehydrogenase, but not with the C-terminal residue of beta-subunit
V180S/E181L
-
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered
V188A
-
ability to be post-translationally lipoylated remains, far-UV CD spectrum differs from wild-type enzyme
additional information