CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Sorbitol dehydrogenase

Enzyme Information

1.1.1.9
D-xylulose reductase.
based on mapping to UniProt Q00796
Xylitol + NAD(+) = D-xylulose + NADH.
-!- Also acts as an L-erythrulose reductase.
1.1.1.56
Ribitol 2-dehydrogenase.
based on mapping to UniProt Q00796
Ribitol + NAD(+) = D-ribulose + NADH.
1.1.1.4
(R,R)-butanediol dehydrogenase.
based on mapping to UniProt Q00796
(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH.
-!- Also converts diacetyl into acetoin with NADH as reductant.
1.1.1.-
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt Q00796
1.1.1.14
L-iditol 2-dehydrogenase.
based on mapping to UniProt Q00796
L-iditol + NAD(+) = L-sorbose + NADH.
-!- This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. -!- It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. -!- Enzymes from different organisms or tissues display different substrate specificity. -!- The enzyme is specific to NAD(+) and can not use NADP(+).

UniProtKB Entries (1)

Q00796
DHSO_HUMAN
Homo sapiens
Sorbitol dehydrogenase

PDB Structure

PDB 1PL7
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase.
Pauly, T.A., Ekstrom, J.L., Beebe, D.A., Chrunyk, B., Cunningham, D., Griffor, M., Kamath, A., Lee, S.E., Madura, R., Mcguire, D., Subashi, T., Wasilko, D., Watts, P., Mylari, B.L., Oates, P.J., Adams, P.D., Rath, V.L.
Structure