Application | Comment | Organism |
---|---|---|
medicine | due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues | Rhodococcus ruber |
medicine | due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Rhodococcus ruber |
gene encoding hDLDH but excluding the N-terminal 1?35 signal peptide region and containing an N-terminal His6-tag, recombinant expression in Escherichia coli strain BL21(DE3) | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis?Menten kinetics | Rhodococcus ruber | |
additional information | - |
additional information | Michaelis?Menten kinetics | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dihydrolipoamide + NAD+ | Rhodococcus ruber | - |
lipoamide + NADH + H+ | - |
r | |
dihydrolipoamide + NAD+ | Homo sapiens | - |
lipoamide + NADH + H+ | - |
r | |
dihydrolipoamide + NAD+ | Rhodococcus ruber GIN1 | - |
lipoamide + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P09622 | - |
- |
Rhodococcus ruber | - |
- |
- |
Rhodococcus ruber GIN1 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration | Rhodococcus ruber |
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dihydrolipoamide + NAD+ | - |
Rhodococcus ruber | lipoamide + NADH + H+ | - |
r | |
dihydrolipoamide + NAD+ | - |
Homo sapiens | lipoamide + NADH + H+ | - |
r | |
dihydrolipoamide + NAD+ | - |
Rhodococcus ruber GIN1 | lipoamide + NADH + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | - |
Rhodococcus ruber |
homodimer | - |
Homo sapiens |
More | structure homology modeling of rhDLDH | Rhodococcus ruber |
Synonyms | Comment | Organism |
---|---|---|
dihydrolipoamide dehydrogenase | - |
Rhodococcus ruber |
dihydrolipoamide dehydrogenase | - |
Homo sapiens |
hDLDH | - |
Homo sapiens |
rhDLDH | - |
Rhodococcus ruber |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Rhodococcus ruber |
22 | - |
assay at room temperature | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Rhodococcus ruber |
7.5 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
flavin | dependent on | Rhodococcus ruber | |
flavin | dependent on | Homo sapiens | |
NAD+ | - |
Rhodococcus ruber | |
NAD+ | - |
Homo sapiens | |
NADH | - |
Rhodococcus ruber | |
NADH | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | structure homology modeling of rhDLDH using the crystal structure of Mycobacterium tuberculosis DLDH, PDB 2A8X, chain A, as template | Rhodococcus ruber |
physiological function | the enzyme DLDH shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of hDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations. Native DLDH is tethered to the pyruvate dehydrogenase complex by interactions with a mediatory protein, E3 binding protein (E3BP), via a region that overlaps with the putative TiO2?binding site, involving V347, H348, D413, E437, Y438, G439, E443, D444, and R447 | Homo sapiens |
physiological function | the enzyme shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of rhDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations | Rhodococcus ruber |