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Literature summary for 1.8.1.4 extracted from
- The involvement of coordinative interactions in the binding of dihydrolipoamide dehydrogenase to titanium dioxide-Localization of a putative binding site (2017), J. Mol. Recognit., 30, e2617 .
Application
| 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(Commentary)
| 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 [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/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P09622 | - |
- |
| Rhodococcus ruber | - |
- |
- |
| Rhodococcus ruber GIN1 | - |
- |
- |
Purification (Commentary)
| 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 and Products (Substrate)
| 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
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Rhodococcus ruber |
| homodimer | - |
Homo sapiens |
| More | structure homology modeling of rhDLDH | Rhodococcus ruber |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dihydrolipoamide dehydrogenase | - |
Rhodococcus ruber |
| dihydrolipoamide dehydrogenase | - |
Homo sapiens |
| hDLDH | - |
Homo sapiens |
| rhDLDH | - |
Rhodococcus ruber |
Temperature Optimum [°C]
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Rhodococcus ruber |
| 7.5 | - |
assay at | Homo sapiens |
Cofactor
| 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
| 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 |
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