Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.14 - L-iditol 2-dehydrogenase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC1.1.1.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
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+.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
sorbitol dehydrogenase, polyol dehydrogenase, d-sorbitol dehydrogenase, nad-sdh, nad-dependent sorbitol dehydrogenase, glucitol dehydrogenase, mdsdh5, goscr, nad-sorbitol dehydrogenase, pdh-11300, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, L-iditol
-
-
-
-
glucitol dehydrogenase
-
-
-
-
L-iditol 2-dehydrogenase
-
-
-
-
L-iditol dehydrogenase (sorbitol)
-
-
-
-
L-iditol:NAD oxidoreductase
-
-
-
-
L-iditol:NAD+ 5-oxidoreductase
-
-
-
-
NAD+-dependent sorbitol dehydrogenase
-
-
-
-
NAD-dependent sorbitol dehydrogenase
-
-
-
-
NAD-sorbitol dehydrogenase
-
-
-
-
polyol dehydrogenase
-
-
-
-
Protein tms1
-
-
-
-
sorbitol dehydrogenase
additional information
-
enzyme belongs to the family of medium-chain dehydrogenase/reductase proteins
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-iditol + NAD+ = L-sorbose + NADH + H+
show the reaction diagram
ordered catalytic mechanism and substrate binding
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-iditol:NAD+ 2-oxidoreductase
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+.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-21-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose + NADH + H+
D-sorbitol + NAD+
show the reaction diagram
-
-
-
-
?
D-psicose + NADH
?
show the reaction diagram
-
-
-
-
?
D-ribulose + NADH
?
show the reaction diagram
-
-
-
-
?
D-sorbitol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
D-sorbose + NADH
?
show the reaction diagram
-
low activity
-
-
?
D-tagatose + NADH
D-galactitol + NAD+
show the reaction diagram
-
-
-
-
?
D-xylulose + NADH
?
show the reaction diagram
-
-
-
-
?
L-erythrulose + NADH
?
show the reaction diagram
-
-
-
-
?
L-iditol + NAD+
?
show the reaction diagram
-
-
-
-
?
L-sorbose + NADH
?
show the reaction diagram
-
-
-
-
?
sorbitol + NAD+
D-fructose + NADH
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
second step of the polyol pathway of glucose metabolism, important in diabetic disease and hyperglycaemia
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
part of the polyol pathway that interconverts glucose and fructose
-
-
?
sorbitol + NAD+
D-fructose + NADH
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
2-methyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
i.e. SDI-157
CP-642,931
-
a potent and specific sorbitol dehydrogenase inhibitor, rmacokinetics, biomarker pharmacodynamics, and safety analysis, overview. The inhibitor is rapidly absorbed through the oral route and effectively inhibits SDH. However, the drug is not well tolerated due to adverse neuromuscular effects. The inhibitor alters the red blood cell sorbitol dehydrogenase activity after oral administration
additional information
-
drug design, inhibitory compounds
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
140
D-fructose
-
-
34
D-ribulose
-
-
1
D-xylulose
-
-
25
L-erythrulose
-
-
800
L-sorbose
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00025
2-hydroxymethyl-4-(4-N,N-dimethylaminosulfonyl-1-piperazino)pyrimidine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.62
-
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
assay at
9.9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
papilla, inner medulla, cortex
Manually annotated by BRENDA team
additional information
-
SDH expression analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the zinc-finger protein ZAC1 is up-regulated under hypertonic stress and negatively regulates expression of SDH, allowing for accumulation of sorbitol as a compatible organic osmolyte
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHSO_HUMAN
357
0
38325
Swiss-Prot
other Location (Reliability: 3)
A0A6I8PIS1_HUMAN
252
0
27076
TrEMBL
other Location (Reliability: 3)
B4DKI2_HUMAN
278
0
29764
TrEMBL
other Location (Reliability: 2)
V9HW89_HUMAN
357
0
38312
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
155000
-
about
37000
-
4 * 37000, about
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme alone, and in complex with NAD+, or with NADH and inhibitor SDI-158, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution, modelling
purified recombinant enyme, hanging drop vapour diffusion method, 22°C, enzyme is complexed with cofactor NAD+ in a molar ratio 1:6, 0.0025 ml protein solution mixed with 0.002 ml well solution containing 0.1 M Tris, pH 8.6, 0.2 M sodium acetate, 10% PEG 3350, and with 0.0005 ml 30% v/v 2-methyl-2,4-pentanediol, 1 week, X-ray diffraction structure determination and analysis at 2.75 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
loses zinc at lower pH
285892
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
-
50% loss of activity after 2 days, non-purified enzyme in serum
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 2 days, non-purified enzyme in serum
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from Escherichia coli by ammonium sulfate precipitation, anion-exchange and dye affinity cromatography, 23fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
zinc-finger protein ZAC1 is up-regulated under hypertonic stress and negatively regulates expression of SDH
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
target for inhibitor design in hyperglycaemia and diabetes mellitus treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dooley, J.F.; Turnquist, L.J.; Racich, L.
Kinetic determination of serum sorbitol dehydrogenase activity with a centrifugal analyzer
Clin. Chem.
25
2026-2029
1979
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Gerlach, U.; Hiby, W.
Sorbit-Dehydrogenase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
601-606
1974
Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Maret, W.
Human sorbitol dehydrogenase - a secondary alcohol dehydrogenase with distinct pathophysiological roles, pH dependent kinetic studies
Adv. Exp. Med. Biol.
383-393
1996
Homo sapiens
Manually annotated by BRENDA team
Darmanin, C.; Iwata, T.; Carper, D.A.; Sparrow, L.G.; Chung, R.P.; El-Kabbani, O.
Expression, purification and preliminary crystallographic analysis of human sorbitol dehydrogenase
Acta Crystallogr. Sect. D
59
558-560
2003
Homo sapiens
Manually annotated by BRENDA team
El-Kabbani, O.; Darmanin, C.; Chung, R.P.
Sorbitol dehydrogenase: structure, function and ligand design
Curr. Med. Chem.
11
465-476
2004
Ovis aries, Homo sapiens, Mammalia, Rattus norvegicus
Manually annotated by BRENDA team
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.
X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase
Structure
11
1071-1085
2003
Homo sapiens (Q00796), Homo sapiens
Manually annotated by BRENDA team
Lanaspa, M.A.; Andres-Hernando, A.; Rivard, C.J.; Dai, Y.; Li, N.; Berl, T.
ZAC1 is up-regulated by hypertonicity and decreases sorbitol dehydrogenase expression, allowing accumulation of sorbitol in kidney cells
J. Biol. Chem.
284
19974-19981
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Landau, Z.; Novotny, M.J.; Preston, G.M.; Wright, K.; Freeman, T.; Dai, H.; Thompson, J.; Oates, P.J.; Calle, R.A.
Pharmacokinetics, pharmacodynamics, tolerability, and safety of a novel sorbitol dehydrogenase inhibitor in healthy participants
J. Clin. Pharmacol.
50
521-530
2010
Homo sapiens
Manually annotated by BRENDA team