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Search results 301 to 323 out of 323 for Ogdh

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Type Details Score
Protein Coding Gene
MGI:1926170 | Dlst
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913378 | Mrps36
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9D2G2
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
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Protein
Q9CQX8
Organism: Mus musculus/domesticus
Length: 102  
Fragment?: false
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Protein Coding Gene
MGI:107450 | Dld
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
O08749
Organism: Mus musculus/domesticus
Length: 509  
Fragment?: false
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Publication
37742191 | J:342103
First Author: Gao Y
Year: 2023
Journal: Cell Rep
Title: ALKBH5 modulates hematopoietic stem and progenitor cell energy metabolism through m(6)A modification-mediated RNA stability control.
Volume: 42
Issue: 10
Pages: 113163
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Publication
29274570 | J:275096
 
First Author: Chalker J
Year: 2018
Journal: Redox Biol
Title: Characterization of the impact of glutaredoxin-2 (GRX2) deficiency on superoxide/hydrogen peroxide release from cardiac and liver mitochondria.
Volume: 15
Pages: 216-227
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Publication
26936970 | J:239495
First Author: Denton RM
Year: 2016
Journal: Biochem J
Title: Calcium-insensitive splice variants of mammalian E1 subunit of 2-oxoglutarate dehydrogenase complex with tissue-specific patterns of expression.
Volume: 473
Issue: 9
Pages: 1165-78
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Publication
31648943 | J:330411
First Author: Wongkittichote P
Year: 2019
Journal: Mol Genet Metab
Title: Tricarboxylic acid cycle enzyme activities in a mouse model of methylmalonic aciduria.
Volume: 128
Issue: 4
Pages: 444-451
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Protein
A0A0G2JGU0
Organism: Mus musculus/domesticus
Length: 27  
Fragment?: true
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Publication
1554728 | -
First Author: Robien MA
Year: 1992
Journal: Biochemistry
Title: Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli.
Volume: 31
Issue: 13
Pages: 3463-71
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Publication
16442803 | -
First Author: Brautigam CA
Year: 2006
Journal: Structure
Title: Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex.
Volume: 14
Issue: 3
Pages: 611-21
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Publication
24077172 | -
First Author: Kumaran S
Year: 2013
Journal: Molecules
Title: Nuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes--a literature review.
Volume: 18
Issue: 10
Pages: 11873-903
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Protein Domain
IPR004167 | PSBD
Type: Domain
Description: The ubiquitous 2-oxoacid dehydrogenases are a family of very large multienzymecomplexes consisting of multiple copies of at least three enzymes whichcatalyze the oxidative decarboxylation of several different 2-oxoacids,resulting in acyl-CoA products. Members of this family include pyruvatedehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxoacid dehydrogenase (BCDH). The three enzymes assembling to form thesecomplexes are the decarboxylase E1 (called E1p, E1o and E1b in PDH, OGDH andBCDH, respectively), dihydrolipoamide acetyl, succinyl and branched-chaintransferase E2 (E2p, E2o and E2b, respectively) and dihydrolipoamidedehydrogenase E3. The E3 component is identical in all three complexes (PDH,OGDH and BCDH) and catalyzes the same reaction. The structural core of all 2-oxoacid dehydrogenase complexes (ODHc) is formed of multiple copies of E2subunits, with the E1 and E3 subunits bound on the periphery. The E2 componentof the ODHc's of both bacteria and eukaryotes serves as the structural core ofthese multienzyme complexes and is comprised of three types of domains.Starting with the N terminus, there are 1-3 tandem repeated lipoyl domains(LD), followed by a peripheral subunit-binding domain (PSBD)responsible for binding E1/E3 chains. The third domain is the C-terminalcatalytic domain (CD). The individual domains are separated by long, flexiblelinker regions allowing large movements of the lipoyl domain(s) to enableactive site coupling. The PSBD domain binds E1 or E3, but not bothsimultaneously. The flexible linker allows the PSBD domain (associated witheither E1 or E3) to move quite freely with respect to the core formed E2catalytic domains [, , , , ].The ~35-residue PSBD domain has a compact structure consisting of two short,parallel α-helices (H1 and H2) separated by a loop (L1), a single helicalturn, and a further, less well-ordered loop (L2) (see PDB:1BAL). The compactstructure of the PSBD domain is stabilized mainly by hydrophobic interactions.The interactions between the PSBD domain and E3 are all mediated by chargedside chains, forming an 'electrostatic zipper'. The residues of the PSBDdomain involved in the interactions are all provided by helix H1 of thisdomain. Helix H2 of PSBD does not interact with E3, but may be involved inbinding E1 [, , ].
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Publication
8805537 | -
First Author: Mande SS
Year: 1996
Journal: Structure
Title: Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.
Volume: 4
Issue: 3
Pages: 277-86
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Publication
10966480 | -
 
First Author: Perham RN
Year: 2000
Journal: Annu Rev Biochem
Title: Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
Volume: 69
Pages: 961-1004
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Protein
P53395
Organism: Mus musculus/domesticus
Length: 482  
Fragment?: false
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Protein
A2AWH8
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Protein
A2AWH7
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
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Protein
Q7TND9
Organism: Mus musculus/domesticus
Length: 482  
Fragment?: false
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Protein
Q8BMF4
Organism: Mus musculus/domesticus
Length: 642  
Fragment?: false
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Protein
Q8BKZ9
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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