Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase and Organism(s) Arabidopsis thaliana

for references in articles please use BRENDA:EC2.3.1.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dihydrolipoamide acetyltransferase, dihydrolipoyl transacetylase, lipoate acetyltransferase, dihydrolipoyl acetyltransferase, dhlta, dihydrolipoyl acetyl transferase, dihydrolipoyllysine-residue acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyltransferase, lipoate
-
-
-
-
DHLTA
-
-
-
-
dihydrolipoate acetyltransferase
-
-
-
-
dihydrolipoic transacetylase
-
-
-
-
dihydrolipoyl acetyltransferase
-
-
-
-
E2
-
-
-
-
E2p
-
-
-
-
lipoate acetyltransferase
-
-
-
-
lipoate transacetylase
-
-
-
-
lipoic acetyltransferase
-
-
-
-
lipoic acid acetyltransferase
-
-
-
-
lipoic transacetylase
-
-
-
-
lipoylacetyltransferase
-
-
-
-
myelin-proteolipid O-palmitoyltransferase
-
-
-
-
palmitoyl-CoA:myelin-proteolipid O-palmitoyltransferase
-
-
-
-
thioltransacetylase A
-
-
-
-
transacetylase X
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:enzyme N6-(dihydrolipoyl)lysine S-acetyltransferase
A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-29-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
show the reaction diagram
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.89
-
fusion protein with glutathione S-transferase
4.09
-
after removal of glutathione S-transferase moiety
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ODP21_ARATH
637
0
68862
Swiss-Prot
Mitochondrion (Reliability: 1)
ODP22_ARATH
539
0
58468
Swiss-Prot
Mitochondrion (Reliability: 5)
ODP23_ARATH
539
0
58467
Swiss-Prot
Mitochondrion (Reliability: 5)
ODP24_ARATH
480
0
50080
Swiss-Prot
Chloroplast (Reliability: 1)
ODP25_ARATH
465
0
48307
Swiss-Prot
Chloroplast (Reliability: 5)
A0A178VAA8_ARATH
473
0
51121
TrEMBL
Chloroplast (Reliability: 2)
A0A7G2E0R9_ARATH
539
0
58512
TrEMBL
Mitochondrion (Reliability: 5)
A0A5S9XC59_ARATH
539
0
58454
TrEMBL
Mitochondrion (Reliability: 5)
A0A654F6Y5_ARATH
539
0
58495
TrEMBL
Mitochondrion (Reliability: 4)
A0A178W5Y1_ARATH
539
0
58467
TrEMBL
Mitochondrion (Reliability: 5)
A0A7G2EMC9_ARATH
473
0
51137
TrEMBL
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50080
-
calculation from nucleotide sequence
59000
-
x * 59000, SDS-PAGE, recombinant protein
60000
67000
-
plastid precursor protein, SDS-PAGE
80000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 59000, SDS-PAGE, recombinant protein
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
additional information
-
protein includes a single lipoyl-prosthetic group covalently attached to Lys96. Despite low primary sequence identity with the bacterial enzyme, the plant protein is recognized and modified by Escherichia coli E2 lipoyl-addition system
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion protein with glutathione S-transferase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guan, Y.; Rawsthorne, S.; Scofield, G.; Shaw, P.; Doonan, J.
Cloning and characterization of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana
J. Biol. Chem.
270
5412-5417
1995
Arabidopsis thaliana
Manually annotated by BRENDA team
Mooney, B.P.; Miernyk, J.A.; Randall, D.D.
Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) from Arabidopsis
Plant Physiol.
120
443-452
1999
Arabidopsis thaliana
Manually annotated by BRENDA team
Casteel, J.; Miernyk, J.A.; Thelen, J.J.
Mapping the lipoylation site of Arabidopsis thaliana plastidial dihydrolipoamide S-acetyltransferase using mass spectrometry and site-directed mutagenesis
Plant Physiol. Biochem.
49
1355-1361
2011
Arabidopsis thaliana
Manually annotated by BRENDA team