Literature summary for 1.1.1.14 extracted from

Hellgren, M.; Kaiser, C.; de Haij, S.; Norberg, A.; Hoeoeg, J.O.
A hydrogen-bonding network in mammalian sorbitol dehydrogenase stabilizes the tetrameric state and is essential for the catalytic power (2007), Cell. Mol. Life Sci., 64, 3129-3138.

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Protein Variants

Protein Variants	Comment	Organism
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	Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.17	-	D-xylitol	wild-type, pH 10.0	Rattus norvegicus
0.33	-	D-sorbitol	wild-type, pH 10.0	Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
40000	-	plus 80000, 160000 and 300000, mutant Y110F	Rattus norvegicus
80000	-	plus 160000, 40000 and 300000, mutant Y110F	Rattus norvegicus
160000	-	plus 80000, 40000 and 300000, mutant Y110F	Rattus norvegicus
300000	-	above 300000, wild-type and part of mutant Y110F	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-sorbitol + NAD+	-	Rattus norvegicus	D-fructose + NADH + H+	-	?
D-xylitol + NAD+	-	Rattus norvegicus	?	-	?
ethanol + NAD+	-	Rattus norvegicus	acetaldehyde + NADH	-	?

Subunits

Subunits	Comment	Organism
dimer	plus tetramer and monomer, mutant 110F	Rattus norvegicus
monomer	plus tetramer and monomer, mutant 110F	Rattus norvegicus
More	network of coupled hydrogen bonds holds up the protein interface and tetramer stability	Rattus norvegicus
tetramer	MALDI-TOF, wild-type and part of mutant Y110F	Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.63	-	D-xylitol	wild-type, pH 10.0	Rattus norvegicus
0.71	-	D-sorbitol	wild-type, pH 10.0	Rattus norvegicus

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Release 2023.1 (January 2023)