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Literature summary extracted from

  • Selvaraj, C.; Krishnasamy, G.; Jagtap, S.; Patel, S.; Dhiman, S.; Kim, T.; Singh, S.; Lee, J.
    Structural insights into the binding mode of D-sorbitol with sorbitol dehydrogenase using QM-polarized ligand docking and molecular dynamics simulations (2016), Biochem. Eng. J., 114, 244-256.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.14 D364A the mutant exhibits abolished energy efficiency compared to the wild type enzyme Gluconobacter oxydans
1.1.1.14 H302A the mutant exhibits abolished energy efficiency compared to the wild type enzyme Gluconobacter oxydans
1.1.1.14 M366A the mutant exhibits abolished energy efficiency compared to the wild type enzyme Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.99.21 additional information
-
 additional information protein-ligand molecular docking and thermodynamics, overview Gluconobacter oxydans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.14 membrane
-
 Gluconobacter oxydans 16020
-
1.1.99.21 membrane membrane-bound dehydrogenase Gluconobacter oxydans 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.99.21 53580
-
-
 Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.14 D-sorbitol + acceptor Gluconobacter oxydans
-
 L-sorbose + reduced acceptor
-
 ?
1.1.99.21 D-sorbitol + acceptor Gluconobacter oxydans
-
 L-sorbose + reduced acceptor
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.14 Gluconobacter oxydans Q9KWR5
-
-
1.1.99.21 Gluconobacter oxydans
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.14 D-sorbitol + acceptor
-
 Gluconobacter oxydans L-sorbose + reduced acceptor
-
 ?
1.1.99.21 D-sorbitol + acceptor
-
 Gluconobacter oxydans L-sorbose + reduced acceptor
-
 ?
1.1.99.21 additional information binding mode of D-sorbitol with sorbitol dehydrogenase using QM-polarized ligand docking and molecular dynamics simulations, His302, Met366, and Asp368 actively participate in D-sorbitol binding, H302 directly forms hydrogen bonds with D-sorbitol and the role of His302 is to hold the D-sorbitol, overview Gluconobacter oxydans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.99.21 ? x * 53580, about, sequence calculation Gluconobacter oxydans
1.1.99.21 More structure analysis by QM-polarized ligand docking and molecular dynamics simulations, modelling, overview Gluconobacter oxydans

Synonyms

EC Number Synonyms Comment Organism
1.1.1.14 SDH
-
 Gluconobacter oxydans
1.1.99.21 D-sorbitol dehydrogenase
-
 Gluconobacter oxydans
1.1.99.21 SDH
-
 Gluconobacter oxydans

General Information

EC Number General Information Comment Organism
1.1.99.21 malfunction mutation of His302 results in the denaturation of protein structure and loss of stability Gluconobacter oxydans
1.1.99.21 metabolism membrane-bound D-sorbitol dehydrogenase is involved in the biotransformation of D-sorbitol to L-sorbose Gluconobacter oxydans
1.1.99.21 additional information sequence alignment-based homology modeling using the structure of NAD-bound sorbitol dehydrogenase, EC 1.1.1.14, with UniProt ID Q9KWR5 as template Gluconobacter oxydans