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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.4.4 - 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and Organism(s) Arabidopsis thaliana

for references in articles please use BRENDA:EC1.2.4.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
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
bckdh, bckdhb, bckdha, branched-chain 2-oxo acid dehydrogenase, branched-chain alpha-keto acid dehydrogenase, alpha-ketoacid dehydrogenase, branched-chain alpha-ketoacid dehydrogenase, bckdc, branched-chain alpha-ketoacid dehydrogenase complex, bcka dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-oxoisocaproate dehydrogenase
-
-
-
-
2-oxoisovalerate dehydrogenase (lipoate)
-
-
-
-
alpha-keto-beta-methylvalerate dehydrogenase
-
-
-
-
alpha-ketoisocaproate dehydrogenase
-
-
-
-
alpha-ketoisocaproic dehydrogenase
-
-
-
-
alpha-ketoisocaproic-alpha-keto-beta-methylvaleric dehydrogenase
-
-
-
-
alpha-ketoisovalerate dehydrogenase
-
-
-
-
alpha-oxoisocaproate dehydrogenase
-
-
-
-
BCDH
-
-
-
-
BCKADC
-
-
-
-
BCKDH
BCKDH E1-alpha
-
-
-
-
BCKDH E1-beta
-
-
-
-
BCOAD
-
-
-
-
branched chain keto acid dehydrogenase
-
-
-
-
branched-chain (-2-oxoacid BCD) dehydrogenase
-
-
-
-
branched-chain 2-keto acid dehydrogenase
-
-
-
-
branched-chain 2-oxo acid dehydrogenase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase
-
-
-
-
branched-chain alpha-oxo acid dehydrogenase
-
-
-
-
branched-chain keto acid dehydrogenase
-
-
-
-
branched-chain ketoacid dehydrogenase
-
-
-
-
branched-chain ketoacid dehydrogenase E1
-
-
dehydrogenase, 2-oxoisocaproate
-
-
-
-
dehydrogenase, 2-oxoisovalerate (lipoate)
-
-
-
-
dehydrogenase, branched chain alpha-keto acid
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-2-methylpropanoylating)
Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-05-4
-
9082-72-8
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activity increases when plants are placed in the dark, expression is strongly associated with the progression of leaf senescence
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ODBA2_ARATH
472
0
53214
Swiss-Prot
Chloroplast (Reliability: 5)
ODBB1_ARATH
352
0
38735
Swiss-Prot
Mitochondrion (Reliability: 2)
ODBB2_ARATH
358
0
39419
Swiss-Prot
Mitochondrion (Reliability: 2)
ODBA1_ARATH
472
0
53488
Swiss-Prot
Mitochondrion (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-subunit
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujiki, Y.; Sato, T.; Ito, M.; Watanabe, A.
Isolation and characterization of cDNA clones for the E1beta and E2 subunits of the branched-chain alpha-ketoacid dehydrogenase complex in Arabidopsis
J. Biol. Chem.
275
6007-6013
2000
Arabidopsis thaliana
Manually annotated by BRENDA team
Peng, C.; Uygun, S.; Shiu, S.H.; Last, R.L.
The impact of the branched-chain ketoacid dehydrogenase complex on amino acid homeostasis in Arabidopsis
Plant Physiol.
169
1807-1820
2015
Arabidopsis thaliana
Manually annotated by BRENDA team