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Information on EC 1.1.1.425 - levoglucosan dehydrogenase
for references in articles please use BRENDA:EC1.1.1.425
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.425 levoglucosan dehydrogenase
IUBMB Comments
Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning. This enzyme is present only in bacteria, and has been characterized from Arthrobacter sp. I-552 and Pseudarthrobacter phenanthrenivorans. cf. EC 2.7.1.232, levoglucosan kinase.
The enzyme appears in viruses and cellular organisms
showSynonyms
levoglucosan dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,6-anhydro-beta-D-glucose dehydrogenase
-
-
-
-
Asphe3_10730
LgdA
LgdH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
levoglucosan + NAD+ = 3-dehydrolevoglucosan + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
1,6-anhydro-beta-D-glucopyranose:NAD+ 3-oxidoreductase
Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning. This enzyme is present only in bacteria, and has been characterized from Arthrobacter sp. I-552 and Pseudarthrobacter phenanthrenivorans. cf. EC 2.7.1.232, levoglucosan kinase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
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Substrates: -
Products: -
Products: -
r
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
Bacillus smithii S-2701M
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Substrates: -
Products: -
Products: -
r
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
Substrates: -
Products: -
Products: -
r
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
Substrates: -
Products: -
Products: -
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
Arthrobacter sp. I-552
-
Substrates: -
Products: -
Products: -
?
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
-
Substrates: -
Products: -
Products: -
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
Bacillus smithii S-2701M
-
Substrates: -
Products: -
Products: -
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
Substrates: -
Products: -
Products: -
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
Substrates: -
Products: -
Products: -
r
additional information
?
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Arthrobacter sp. I-552
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Substrates: the reaction follows a sequential mechanism. Catalytic activity is specific for levoglucosan and NAD+. Poor substrates: ribose and glucose
Products: -
Products: -
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additional information
?
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Arthrobacter sp. I-552
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Substrates: the reaction follows a sequential mechanism. Catalytic activity is specific for levoglucosan and NAD+. Poor or no substrates: ribose and glucose, mannose, galactose, fructose, fucose, rhamnose, galactosan, sedoheptulosan
Products: -
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additional information
?
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Substrates: about 4% of the activity with levoglucosan with L-sorbose and 1,5-anhydro-D-glucitol
Products: -
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additional information
?
-
-
Substrates: about 4% of the activity with levoglucosan with L-sorbose and 1,5-anhydro-D-glucitol
Products: -
Products: -
-
additional information
?
-
Substrates: about 4% of the activity with levoglucosan with L-sorbose and 1,5-anhydro-D-glucitol
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Arthrobacter sp. I-552
-
Substrates: the reaction follows a sequential mechanism. Catalytic activity is specific for levoglucosan and NAD+. Poor substrates: ribose and glucose
Products: -
Products: -
-
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
-
Substrates: -
Products: -
Products: -
r
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
Bacillus smithii S-2701M
-
Substrates: -
Products: -
Products: -
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
Arthrobacter sp. I-552
-
Substrates: -
Products: -
Products: -
?
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
-
Substrates: -
Products: -
Products: -
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
Bacillus smithii S-2701M
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Arthrobacter sp. I-552
-
not inhibitory at 1 mM: Mg2+, Ca2+, K+, Na+, iodoacetic acid, EDTA, o-phenanthroline, ferricyanide
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.65
substrate 1,5-anhydro-D-glucitol, pH 8.5, 40°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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
metabolism
metabolism
-
in the metabolic pathway from levoglucosan to glucose, LgdA (LGDH) catalyzes 3-dehydrogenation of levoglucosan to produce 3-keto-levoglucosan, which undergoes beta-elimination of 3-keto-levoglucosan by LgdB1, followed by hydration to produce 3-keto-D-glucose by LgdB2. Next, LgdC reduces 3-keto-D-glucose to glucose
metabolism
Bacillus smithii S-2701M
-
in the metabolic pathway from levoglucosan to glucose, LgdA (LGDH) catalyzes 3-dehydrogenation of levoglucosan to produce 3-keto-levoglucosan, which undergoes beta-elimination of 3-keto-levoglucosan by LgdB1, followed by hydration to produce 3-keto-D-glucose by LgdB2. Next, LgdC reduces 3-keto-D-glucose to glucose
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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). F0M433_PSEPM
Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG 23796 / Sphe3)
390
0
42118
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
4 * 42000, SDS-PAGE, 4 * 44280, calculated from sequence
tetramer
-
4 * 42000, SDS-PAGE, 4 * 44280, calculated from sequence
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of LgdH in the apo and complex forms with NADH, NADH plus levoglucosan, and NADH plus L-sorbose. LgdH has a typical fold of Gfo/Idh/MocA family proteins. The active site recognizes the levoglucosan molecule with six hydrogen bonds, and the C3 atom of levoglucosan is closely located to the C4 atom of NADH nicotinamide
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakahara, K.; Kitamura, Y.; Yamagishi, Y.; Shoun, H.; Yasui, T.
Levoglucosan dehydrogenase involved in the assimilation of levoglucosan in Arthrobacter sp. I-552
Biosci. Biotechnol. Biochem.
58
2193-2196
1994
Arthrobacter sp. I-552
brenda
Sugiura, M.; Nakahara, M.; Yamada, C.; Arakawa, T.; Kitaoka, M.; Fushinobu, S.
Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase
J. Biol. Chem.
293
17375-17386
2018
Pseudarthrobacter phenanthrenivorans (F0M433), Pseudarthrobacter phenanthrenivorans, Pseudarthrobacter phenanthrenivorans DSM 18606 (F0M433)
brenda
Kuritani, Y.; Sato, K.; Dohra, H.; Umemura, S.; Kitaoka, M.; Fushinobu, S.; Yoshida, N.
Conversion of levoglucosan into glucose by the coordination of four enzymes through oxidation, elimination, hydration, and reduction
Sci. Rep.
10
20066
2020
Bacillus smithii, Bacillus smithii S-2701M
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.425)
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Release 2023.1 (January 2023)
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