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Literature summary extracted from

  • Dayan, A.; Babin, G.; Ganoth, A.; Kayouf, N.S.; Nitoker Eliaz, N.; Mukkala, S.; Tsfadia, Y.; Fleminger, G.
    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 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.8.1.4 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
1.8.1.4 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)

EC Number Cloned (Comment) Organism
1.8.1.4 DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Rhodococcus ruber
1.8.1.4 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.4 additional information
-
 additional information Michaelis?Menten kinetics Rhodococcus ruber
1.8.1.4 additional information
-
 additional information Michaelis?Menten kinetics Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+ Rhodococcus ruber
-
 lipoamide + NADH + H+
-
 r
1.8.1.4 dihydrolipoamide + NAD+ Homo sapiens
-
 lipoamide + NADH + H+
-
 r
1.8.1.4 dihydrolipoamide + NAD+ Rhodococcus ruber GIN1
-
 lipoamide + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Homo sapiens P09622
-
-
1.8.1.4 Rhodococcus ruber
-
-
-
1.8.1.4 Rhodococcus ruber GIN1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration Rhodococcus ruber
1.8.1.4 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
 Rhodococcus ruber lipoamide + NADH + H+
-
 r
1.8.1.4 dihydrolipoamide + NAD+
-
 Homo sapiens lipoamide + NADH + H+
-
 r
1.8.1.4 dihydrolipoamide + NAD+
-
 Rhodococcus ruber GIN1 lipoamide + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.8.1.4 homodimer
-
 Rhodococcus ruber
1.8.1.4 homodimer
-
 Homo sapiens
1.8.1.4 More structure homology modeling of rhDLDH Rhodococcus ruber

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Rhodococcus ruber
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Homo sapiens
1.8.1.4 hDLDH
-
 Homo sapiens
1.8.1.4 rhDLDH
-
 Rhodococcus ruber

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.4 22
-
 assay at room temperature Rhodococcus ruber
1.8.1.4 22
-
 assay at room temperature Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.4 7.5
-
 assay at Rhodococcus ruber
1.8.1.4 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 flavin dependent on Rhodococcus ruber
1.8.1.4 flavin dependent on Homo sapiens
1.8.1.4 NAD+
-
 Rhodococcus ruber
1.8.1.4 NAD+
-
 Homo sapiens
1.8.1.4 NADH
-
 Rhodococcus ruber
1.8.1.4 NADH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.8.1.4 additional information structure homology modeling of rhDLDH using the crystal structure of Mycobacterium tuberculosis DLDH, PDB 2A8X, chain A, as template Rhodococcus ruber
1.8.1.4 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
1.8.1.4 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