1.1.1.14: L-iditol 2-dehydrogenase

This is an abbreviated version, for detailed information about L-iditol 2-dehydrogenase, go to the full flat file.

Reaction

L-Iditol
+
NAD+
=
L-sorbose
+
NADH
+
H+

Synonyms

ADH, D-sorbitol dehydrogenase, dehydrogenase, L-iditol, Dgeo_2865, glucitol dehydrogenase, Hxt13, Hxt15, Hxt16, Hxt17, L-iditol 2-dehydrogenase, L-iditol dehydrogenase (sorbitol), L-iditol:NAD oxidoreductase, L-iditol:NAD+ 5-oxidoreductase, LeSDH, MdSDH5, More, NAD+-dependent sorbitol dehydrogenase, NAD-dependent polyol dehydrogenase, NAD-dependent sorbitol dehydrogenase, NAD-SDH, NAD-sorbitol dehydrogenase, PDH-11300, polyol dehydrogenase, Protein tms1, SDH, SldA, SLDH, SOR, Sor1, Sor2, sorbitol dehydrogenase, sorbitol dehydrogenase 1, sorbitol dehydrogenase 2, sorbitol transporter, SORD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.14 L-iditol 2-dehydrogenase

Engineering

Engineering on EC 1.1.1.14 - L-iditol 2-dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E154C
-
purified preparations of mutant contain 0.1-0.4 atoms of Zn2+ per subunit and exhibit a constant catalytic Zn2+ centre activity of 1.19 per s, mutant does not require exogenous Zn2+ for stability. Mutant retains less than 1% of wild-type catalytic efficiency and displays similar primary and solvent deuterium effects as wild-type
D364A
the mutant exhibits abolished energy efficiency compared to the wild type enzyme
H302A
the mutant exhibits abolished energy efficiency compared to the wild type enzyme
M366A
the mutant exhibits abolished energy efficiency compared to the wild type enzyme
Y110F
-
mutation in hydrogen onding network, complete loss of activity and destabilization of protein into tetramers, dimers and monomers compared to only tetramers for wild-type
additional information