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Literature summary extracted from

  • Hiromasa, Y.; Yan, X.; Roche, T.E.
    Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r (2008), Biochemistry, 47, 2312-2324.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.2.1.17 medicine ECHS1 down-regulation contributes to high-fat diet-induced hepatic steatosis Mus musculus
4.2.1.17 medicine ECHS1 down-regulation contributes to high-fat diet-induced hepatic steatosis Homo sapiens
4.2.1.17 medicine ECHS1 down-regulation contributes to high-fat diet-induced hepatic steatosis Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.12 inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase is expressed as a GST fusion protein Homo sapiens
2.3.1.122 expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium avium
2.3.1.122 expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium leprae
2.3.1.136 expressed in Escherichia coli as a C-terminal hexahistidine tagged fusion protein Neisseria meningitidis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.122 L130S leucine at position 130 of Mycobacterium leprae FbpA limits access of mycolate-containing glycolipid substrates to their binding site. Mutant L130S exhibits an enhanced mycosyltransferase activity compared to wild-type while the ability to transfer the unbranched acyl chain is unchanged. Km (substrate: short-chain trehalose monomycolate): 0.043 mM, sharply decreased compared to wild-type Mycobacterium leprae
2.3.1.122 S130L mutant S130L of Mycobacterium avium exhibits a reduced mycosyltransferase activity compared to wild-type Mycobacterium avium
2.3.1.136 D359A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 D371A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 D376A mutant shows no enzymatic activity Neisseria meningitidis
2.3.1.136 DELTA1-103 mutant lacking the first 103 amino acids: after purification mutant is found as a monomer, indicating that dimerization of OatC depends on the first 34 amino acids. Mutant shows no activity Neisseria meningitidis
2.3.1.136 DELTA1-34 mutant lacking the first 34 amino acids: after purification mutant is found as a monomer, indicating that dimerization of OatC depends on the first 34 amino acids. Mutant retains 25% activity Neisseria meningitidis
2.3.1.136 E336A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 E345A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 E379A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 H111A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 H183A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 H267A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 H31A mutant shows enzymatic activity comparable to wild-type Neisseria meningitidis
2.3.1.136 H399A mutant shows no enzymatic activity Neisseria meningitidis
2.3.1.136 H456A mutant shows reduced enzymatic activity, 70% of wild-type level Neisseria meningitidis
2.3.1.136 S285A mutant retains 80% of wild-type activity Neisseria meningitidis
2.3.1.136 S286A mutant shows no enzymatic activity Neisseria meningitidis
2.3.1.136 S286C mutant shows no enzymatic activity Neisseria meningitidis
2.5.1.15 P57S the prevalence of DHPS mutations in Pneumocystis jirovecii strains isolated from South African Pneumocystis jirovecii pneumonia patients are examined. Mutations resulting in amino-acid substitutions Thr55Ala and/or Pro57Ser are detected in Pneumocystis jirovecii from 85/151 (56%) patients. The high frequency of PCP episodes with Pneumocystis jirovecii harbouring DHPS mutations in South Africa indicates that populations of this fungus are evolving under considerable selective pressure exerted by sulfa-containing antibiotics Pneumocystis jirovecii
2.5.1.15 T55A the prevalence of DHPS mutations in Pneumocystis jirovecii strains isolated from South African Pneumocystis jirovecii pneumonia patients are examined. Mutations resulting in amino-acid substitutions Thr55Ala and/or Pro57Ser are detected in Pneumocystis jirovecii from 85/151 (56%) patients. The high frequency of PCP episodes with Pneumocystis jirovecii harbouring DHPS mutations in South Africa indicates that populations of this fungus are evolving under considerable selective pressure exerted by sulfa-containing antibiotics Pneumocystis jirovecii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.122 0.043
-
 alpha,alpha-trehalose 6-monomycolate mutant L130S, short-chain trehalose monomycolate is used as a substrate, Vmax: 4.27 nmol/min/nmol Mycobacterium leprae
2.3.1.122 0.459
-
 alpha,alpha-trehalose 6-monomycolate wild-type, short-chain trehalose monomycolate is used as a substrate, Vmax: 3.83 nmol/min/nmol Mycobacterium leprae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.12 K+ association of the pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase (E2)) dimers is enhanced by K+ Homo sapiens
2.3.1.12 phosphate phosphate has a pronounced effect in increasing ligand interference with pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase (E2)) Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.136 54000
-
 SDS-PAGE, the first 34 amino acids form an efficient oligomerization domain, 2 * 54000 Da Neisseria meningitidis
2.3.1.136 54300
-
 SDS-PAGE Neisseria meningitidis
2.3.1.136 105000
-
 gel filtration Neisseria meningitidis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.12 Homo sapiens
-
-
-
2.3.1.15 Mus musculus
-
-
-
2.3.1.122 Mycobacterium avium
-
-
-
2.3.1.122 Mycobacterium leprae
-
-
-
2.3.1.136 Neisseria meningitidis
-
-
-
2.5.1.15 Pneumocystis jirovecii
-
-
-
4.2.1.17 Homo sapiens
-
-
-
4.2.1.17 Mus musculus
-
-
-
4.2.1.17 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.122 using Ni-NTA chromatography Mycobacterium avium
2.3.1.122 using Ni-NTA chromatography Mycobacterium leprae
2.3.1.136 using a HisTrap HP column and a a Superdex 200 HR 10/30 column. FInal yield: 24 mg of enzyme from 500 ml of bacterial culture Neisseria meningitidis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.17 AML-12 cell
-
 Mus musculus
-
4.2.1.17 liver
-
 Mus musculus
-
4.2.1.17 liver
-
 Homo sapiens
-
4.2.1.17 liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.122 additional information
-
 compared to FbpA of Mycobacterium leprae activity of FbpA is strikingly enhanced in Mycobacterium avium Mycobacterium avium
2.3.1.122 additional information
-
 compared to FbpA of Mycobacterium tuberculosis and Mycobacterium avium activity of FbpA is reduced in Mycobacterium leprae Mycobacterium leprae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.122 2 alpha,alpha-trehalose 6-monomycolate
-
 Mycobacterium avium alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
-
 ?
2.3.1.122 2 alpha,alpha-trehalose 6-monomycolate substrate contains alpha-branched long-chain fatty acids. Only tiny amounts of trehalose dimycolate are detected. It is shown that FbpA mycolyltransferase from Mycobacterium leprae retains the ability to transfer unbranched but not alpha-branched fatty acids Mycobacterium leprae alpha,alpha-trehalose 6,6'-dimycolate + alpha,alpha-trehalose
-
 ?
2.3.1.122 alpha,alpha-trehalose monomycolate + D-glucose D-glucose is used as an alternative acceptor substrate. FbpA mycolyltransferase from Mycobacterium leprae shows only trace of glucose monomycolate is detected Mycobacterium leprae D-glucose monomycolate + alpha,alpha-trehalose
-
 ?
2.3.1.122 alpha,alpha-trehalose monomycolate + D-glucose Mycobacterium tuberculosis and Mycobacterium avium, replace TDM with glucose monomycolate by borrowing host-derived glucose as an alternative substrate for the FbpA mycolyltransferase Mycobacterium avium D-glucose monomycolate + alpha,alpha-trehalose
-
 ?
2.3.1.136 additional information no enzymatic activity is detected for free Neu5Ac and CMP-Neu5Ac, indicating that OatC is specific for oligo- or polySia. Since only Neisseria meningitidis serogroup C capsular polysaccharide (NmC-CPS) serves as an acceptor, this demonstrates that OatC is highly specific for alpha2,9-linked polySia Neisseria meningitidis ?
-
 ?
2.3.1.136 Neisseria meningitidis serogroup C capsular polysaccharide + acetyl-CoA relative activity: 100% Neisseria meningitidis ?
-
 ?
2.3.1.136 Neisseria meningitidis serogroup C capsular polysaccharide + propionyl-CoA relative activity: 21.4% Neisseria meningitidis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.12 dimer GST-L2, glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase exists as a dimer Homo sapiens
2.3.1.136 homodimer SDS-PAGE, the first 34 amino acids form an efficient oligomerization domain, 2 * 54000 Da Neisseria meningitidis

Synonyms

EC Number Synonyms Comment Organism
2.3.1.12 dihydrolipoyl acetyltransferase glutathione-S-transferase fused to the inner lipoyl domain is used Homo sapiens
2.3.1.15 glycerol-3-phosphate acyltransferase-1
-
 Mus musculus
2.3.1.15 GPAT-1
-
 Mus musculus
2.3.1.122 FbpA mycolyltransferase
-
 Mycobacterium avium
2.3.1.122 FbpA mycolyltransferase
-
 Mycobacterium leprae
2.3.1.136 OatC
-
 Neisseria meningitidis
2.3.1.136 polysialic-acid O-acetyltransferase
-
 Neisseria meningitidis
2.5.1.15 DHPS
-
 Pneumocystis jirovecii
2.5.1.15 dihydropteroate synthase
-
 Pneumocystis jirovecii
4.2.1.17 ECHS1
-
 Mus musculus
4.2.1.17 ECHS1
-
 Homo sapiens
4.2.1.17 ECHS1
-
 Rattus norvegicus
4.2.1.17 enoyl-CoA hydratase
-
 Mus musculus
4.2.1.17 enoyl-CoA hydratase
-
 Homo sapiens
4.2.1.17 enoyl-CoA hydratase
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.122 37
-
 assay at Mycobacterium avium
2.3.1.122 37
-
 assay at Mycobacterium leprae
2.3.1.136 25
-
 assay at Neisseria meningitidis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.122 7.5
-
 assay at Mycobacterium avium
2.3.1.122 7.5
-
 assay at Mycobacterium leprae
2.3.1.136 7.5
-
 assay at Neisseria meningitidis

Expression

EC Number Organism Comment Expression
4.2.1.17 Rattus norvegicus a proteomic approach is applied to examine the effect of high fat diet on the liver proteome during the progression of nonalcoholic fatty liver disease. Male rats fed an high-fat diet for 4, 12, and 24 weeks show a reduced protein level of ECHS1 down
4.2.1.17 Homo sapiens ECHS1 expression level in patients with simple steatosis is reduced down

General Information

EC Number General Information Comment Organism
2.3.1.12 malfunction Nov3r a lipoyl group-binding site inhibitor (related trifluoro-2-hydroxy-2-menthylpropionate compound) prevents pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase) binding and dissect the effects of Nov3r binding at the lipoyl group binding site on PDHK2 binding of other ligands Homo sapiens
2.3.1.15 malfunction T-lymphocyte proliferation is inhibited and activation induced apoptosis is increased in GPAT-1 knockout mice. Th-1 (IL-2 and IFN-gamma) cytokine secretion is reduced, and Th-2 (IL-4 and IL-10) cytokine secretion is increased. An increased arachidonate content and subsequent increased prostaglandin E2 secretion is shown in knockout mice, which may inhibit T-lymphocyte proliferation Mus musculus
2.5.1.15 physiological function the prevalence of DHPS mutations in Pneumocystis jirovecii strains isolated from South African Pneumocystis jirovecii pneumonia patients are examined. Mutations resulting in amino-acid substitutions Thr55Ala and/or Pro57Ser are detected in Pneumocystis jirovecii from 85/151 (56%) patients. The high frequency of PCP episodes with Pneumocystis jirovecii harbouring DHPS mutations in South Africa indicates that populations of this fungus are evolving under considerable selective pressure exerted by sulfa-containing antibiotics Pneumocystis jirovecii
4.2.1.17 malfunction siRNA-mediated knockdown of ECHS1 in the murine hepatocyte cell line alpha mouse liver 12 demonstrate increased cellular lipid accumulation induced by free fatty acid overload. Administering ECHS1 siRNA specifically reduces the expression of ECHS1 protein in mice liver, which significantly exacerbates the hepatic steatosis induced by an high fat diet Mus musculus