Any feedback?
No. of entries
Information on EC 1.1.1.370 - scyllo-inositol 2-dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.370
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.370 scyllo-inositol 2-dehydrogenase (NAD+)
IUBMB Comments
The enzyme, found in the bacterium Bacillus subtilis, has no activity with NADP+ [cf. EC 1.1.1.371, scyllo-inositol 2-dehydrogenase (NADP+)]. It is part of a scyllo-inositol degradation pathway leading to acetyl-CoA.
The enzyme appears in viruses and cellular organisms
- 1.1.1.370
- myo-inositols
-
stereoisomer
- scyllo-inosose
- repressor
-
gymnema
-
terrae
-
burkholderia
-
paracoccus
-
casei
- l-glucose
-
honeydew
- lactobacillus
- nicotinamide
-
1-dehydrogenase
- honey
-
stereoselectively
-
sylvestre
- 2-deoxy-scyllo-inosose
showSynonyms
scyllo-inositol dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DegA
IolX
NAD+-dependent SI dehydrogenase
yisS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
scyllo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
myo-, chiro- and scyllo-inositol degradation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
scyllo-inositol:NAD+ 2-oxidoreductase
The enzyme, found in the bacterium Bacillus subtilis, has no activity with NADP+ [cf. EC 1.1.1.371, scyllo-inositol 2-dehydrogenase (NADP+)]. It is part of a scyllo-inositol degradation pathway leading to acetyl-CoA.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-epi-2-inosose + NADH + H+
myo-inositol + NAD+
Substrates: -
Products: -
Products: -
r
myo-inositol + NAD+
L-epi-2-inosose + NADH + H+
Substrates: -
Products: -
Products: -
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
Products: -
Products: -
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: no activity with NADP+
Products: 2,4,6/3,5-pentahydroxycyclohexanone i.e. (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone i.e. scyllo-inosose
Products: 2,4,6/3,5-pentahydroxycyclohexanone i.e. (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone i.e. scyllo-inosose
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
Products: -
?
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
Products: -
Products: -
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: no activity with NADP+
Products: 2,4,6/3,5-pentahydroxycyclohexanone i.e. (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone i.e. scyllo-inosose
Products: 2,4,6/3,5-pentahydroxycyclohexanone i.e. (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone i.e. scyllo-inosose
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
Products: -
?
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
Products: -
r
scyllo-inositol + NAD+
scyllo-inosose + NADH + H+
Substrates: -
Products: -
Products: -
r
scyllo-inositol + NAD+
scyllo-inosose + NADH + H+
Substrates: -
Products: -
Products: -
r
scyllo-inosose + NADH + H+
scyllo-inositol + NAD+
Substrates: -
Products: -
Products: -
r
scyllo-inosose + NADH + H+
scyllo-inositol + NAD+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: the enzyme performs also reversible L-glucose oxidation, structural basis and kinetics, overview. Substrate binding structures, detailed overview. Pl-scyllo-IDH has a different regioselectivity compared to myo-IDH toward myo-inositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme performs also reversible L-glucose oxidation, structural basis and kinetics, overview. Substrate binding structures, detailed overview. Pl-scyllo-IDH has a different regioselectivity compared to myo-IDH toward myo-inositol
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-epi-2-inosose + NADH + H+
myo-inositol + NAD+
Substrates: -
Products: -
Products: -
r
myo-inositol + NAD+
L-epi-2-inosose + NADH + H+
Substrates: -
Products: -
Products: -
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
Products: -
Products: -
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
Products: -
?
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
Products: -
Products: -
r
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
Products: -
?
scyllo-inositol + NAD+
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Substrates: -
Products: -
Products: -
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
cofactor binding mode and structure analysis, overview
-
additional information
-
cofactor binding mode and structure analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
40.3
L-epi-2-inosose
pH 6.0, 25°C, recombinant wild-type enzyme
53.3
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
3.7
scyllo-Inositol
pH 9.0, 25°C, recombinant wild-type enzyme
40.6
scyllo-Inositol
pH 9.0, 25°C, recombinant mutant R178A
154
scyllo-Inositol
pH 9.0, 25°C, recombinant mutant H318A
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
75
L-epi-2-inosose
pH 6.0, 25°C, recombinant wild-type enzyme
9.53
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
1.43
scyllo-Inositol
pH 9.0, 25°C, recombinant mutant H318A
8.1
scyllo-Inositol
pH 9.0, 25°C, recombinant mutant R178A
11.75
scyllo-Inositol
pH 9.0, 25°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.86
L-epi-2-inosose
pH 6.0, 25°C, recombinant wild-type enzyme
0.18
myo-inositol
pH 9.0, 25°C, recombinant wild-type enzyme
0.0093
scyllo-Inositol
pH 9.0, 25°C, recombinant mutant H318A
0.2
scyllo-Inositol
pH 9.0, 25°C, recombinant mutant R178A
3.18
scyllo-Inositol
pH 9.0, 25°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glucose-fructose oxidase/inositol dehydrogenase/microbial rhizopine-catabolizing (GFO/IDH/MocA) family
malfunction
metabolism
physiological function
additional information
malfunction
inactivation of iolX impairs growth with scyllo-inositol as the carbon source
malfunction
-
inactivation of iolX impairs growth with scyllo-inositol as the carbon source
-
metabolism
the enzyme is involved in the inositol metabolic pathway in Bacillus subtilis, organization of the relevant genes, overview
metabolism
scyllo-inositol dehydrogenase is involved in the first step in the pathway that oxidizes L-glucose to produce L-glucono-1,5-lactone with concomitant reduction of NAD+ dependent manner
metabolism
-
the enzyme is involved in the inositol metabolic pathway in Bacillus subtilis, organization of the relevant genes, overview
-
physiological function
the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
physiological function
Bacillus subtilis is able to utilize at least three inositol stereoisomers as carbon sources, myo-, scyllo-, and D-chiro-inositol (MI, SI, and DCI, respectively). NAD+-dependent SI dehydrogenase is responsible for SI catabolism. IolQ is a transcriptional repressor of iolX. Expression of gene iolQ is required to regulate gene iolX transcription in response to scyllo-inositol, identification of the two IolQ-binding sites within the iolX promoter region
physiological function
-
the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA
-
physiological function
-
Bacillus subtilis is able to utilize at least three inositol stereoisomers as carbon sources, myo-, scyllo-, and D-chiro-inositol (MI, SI, and DCI, respectively). NAD+-dependent SI dehydrogenase is responsible for SI catabolism. IolQ is a transcriptional repressor of iolX. Expression of gene iolQ is required to regulate gene iolX transcription in response to scyllo-inositol, identification of the two IolQ-binding sites within the iolX promoter region
-
additional information
in addition to the conserved catalytic residues (Lys106, Asp191, and His195), another residue, His318, located in the loop region of the adjacent subunit, is involved in substrate recognition. The Arg178 residue located in the flexible loop at the entrance of the catalytic site is also involved in substrate recognition, and plays an important role in accepting both L-glucose and inositols as substrates. The corresponding distances in the myo-inositol and scyllo-inosose complexes are 2.8 A and 3.1 A, respectively, and the relative positions of NAD+ and the inositols are the same as those seen in the lactone complex
additional information
-
in addition to the conserved catalytic residues (Lys106, Asp191, and His195), another residue, His318, located in the loop region of the adjacent subunit, is involved in substrate recognition. The Arg178 residue located in the flexible loop at the entrance of the catalytic site is also involved in substrate recognition, and plays an important role in accepting both L-glucose and inositols as substrates. The corresponding distances in the myo-inositol and scyllo-inosose complexes are 2.8 A and 3.1 A, respectively, and the relative positions of NAD+ and the inositols are the same as those seen in the lactone complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). IOLX_BACSU
Bacillus subtilis (strain 168)
342
0
37484
Swiss-Prot
Secretory Pathway (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
one Pl-scyllo-IDH subunit contains two domains. The N-terminal domain adopted a Rossmann fold motif for the binding of NAD+, and the C-terminal domain bound substrate. The C-terminal domain contains a large beta-sheet composed of 8 parallel and anti-parallel beta-strands. A long loop extending from G303-G321 is found here to be a characteristic feature of Pl-scyllo-IDH. This loop is involved in subunit interactions, as well as substrate recognition in the adjacent subunit, as described below. Other interactions involved in oligomer formation are mainly mediated by the 8-stranded beta-sheet in the C-terminal domain
additional information
-
one Pl-scyllo-IDH subunit contains two domains. The N-terminal domain adopted a Rossmann fold motif for the binding of NAD+, and the C-terminal domain bound substrate. The C-terminal domain contains a large beta-sheet composed of 8 parallel and anti-parallel beta-strands. A long loop extending from G303-G321 is found here to be a characteristic feature of Pl-scyllo-IDH. This loop is involved in subunit interactions, as well as substrate recognition in the adjacent subunit, as described below. Other interactions involved in oligomer formation are mainly mediated by the 8-stranded beta-sheet in the C-terminal domain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified His-tagged wild-type and selenomethionine-labeled enzyme in apoform and in a ternary complex with NAD+ and L-glucono-1,5-lactone, and in complex with myo-inositol and scyllo-inosose, hanging-drop vapor-diffusion method, mixing of 0.002 ml of protein solution with 0.02 ml of reservoir solution containing 0.1 M sodium acetate pH 4.8, and 12% PEG 3350, 20°C, crystals are soaked for one minute with 25 mM of NAD+ and 100 mM substrate in the reservoir solution, X-ray diffraction structure deteramintion and analysis at 1.75-2.3 A resolution, the structures complexed with myo-inositol/NAD+ and scyllo-inosose/NAD+ are solved at 2.3 A and 2.0 A resolution, respectively. Molecular replacement using the Se-Met-structure as the search model, modeling. The crystal is soaked with L-glucose and the resulting structure is determined
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H318A
site-directed mutagenesis, the kcat value for scyllo-inositol decreases resulting in a very weak activity compared to wild-type enzyme
R178A
site-directed mutagenesis, the mutation increases the Km value by 10fold compared to wild-type and decreases the kcat value for scyllo-inositol as a substrate, the mutant shows reduced activity
additional information
additional information
construction of an iolX disruption mutant strain BFS3018 from wild-type strain 168
additional information
-
construction of an iolX disruption mutant strain BFS3018 from wild-type strain 168
additional information
-
construction of an iolX disruption mutant strain BFS3018 from wild-type strain 168
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a C-terminally His6-tagged fusion protein
gene lgdA, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strains BL21(DE3) or B834(DE3), the latter results in expression of a selenomethionine-labeled enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme is prominently expressed when Bacillus subtilis is grown on medium containing scyllo-inositol
gene iolQ encodes a repressor of the iolX transcription, gene iolQ is organized in an operon immediately upstream of iolX, the repressor binds to the promoter region of iolX
induced during growth on scyllo-inositol
myo- and scyllo-inositol are intracellular inducers of gene iolX, but they fail to antagonize DNA binding of IolQ in in vitro experiments
enzyme is prominently expressed when Bacillus subtilis is grown on medium containing scyllo-inositol
enzyme is prominently expressed when Bacillus subtilis is grown on medium containing scyllo-inositol
-
-
gene iolQ encodes a repressor of the iolX transcription, gene iolQ is organized in an operon immediately upstream of iolX, the repressor binds to the promoter region of iolX
gene iolQ encodes a repressor of the iolX transcription, gene iolQ is organized in an operon immediately upstream of iolX, the repressor binds to the promoter region of iolX
-
-
myo- and scyllo-inositol are intracellular inducers of gene iolX, but they fail to antagonize DNA binding of IolQ in in vitro experiments
myo- and scyllo-inositol are intracellular inducers of gene iolX, but they fail to antagonize DNA binding of IolQ in in vitro experiments
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morinaga, T.; Ashida, H.; Yoshida, K.
Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis
Microbiology
156
1538-1546
2010
Bacillus subtilis (P40332), Bacillus subtilis 168 (P40332)
brenda
Kang, D.; Michon, C.; Morinaga, T.; Tanaka, K.; Takenaka, S.; Ishikawa, S.; Yoshida, K.
Bacillus subtilis IolQ (DegA) is a transcriptional repressor of iolX encoding NAD+-dependent scyllo-inositol dehydrogenase
BMC Microbiol.
17
154
2017
Bacillus subtilis (P40332), Bacillus subtilis, Bacillus subtilis 168 (P40332)
brenda
Fukano, K.; Ozawa, K.; Kokubu, M.; Shimizu, T.; Ito, S.; Sasaki, Y.; Nakamura, A.; Yajima, S.
Structural basis of L-glucose oxidation by scyllo-inositol dehydrogenase implications for a novel enzyme subfamily classification
PLoS ONE
13
e0198010
2018
Paracoccus laeviglucosivorans (K7ZP76), Paracoccus laeviglucosivorans
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.370)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
