BRENDA home
History
Enzyme Nomenclature
Information on EC 1.1.1.425 - levoglucosan dehydrogenase
for references in articles please use BRENDA:EC1.1.1.425Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.425 levoglucosan dehydrogenaseIUBMB 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.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,6-anhydro-beta-D-glucose dehydrogenase
-
-
-
-
Asphe3_10730
LgdA
LgdH
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
levoglucosan + NAD+ = 3-dehydrolevoglucosan + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
-
-
-
r
3-dehydrolevoglucosan + NADH + H+
levoglucosan + NAD+
-
-
-
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
-
-
-
r
levoglucosan + NAD+
3-dehydrolevoglucosan + NADH + H+
-
-
-
r
additional information
?
-
Arthrobacter sp. I-552
-
the reaction follows a sequential mechanism. Catalytic activity is specific for levoglucosan and NAD+. Poor substrates: ribose and glucose
-
-
-
additional information
?
-
Arthrobacter sp. I-552
-
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
-
-
-
additional information
?
-
about 4% of the activity with levoglucosan with L-sorbose and 1,5-anhydro-D-glucitol
-
-
-
additional information
?
-
-
about 4% of the activity with levoglucosan with L-sorbose and 1,5-anhydro-D-glucitol
-
-
-
additional information
?
-
about 4% of the activity with levoglucosan with L-sorbose and 1,5-anhydro-D-glucitol
-
-
-
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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Arthrobacter sp. I-552
-
the reaction follows a sequential mechanism. Catalytic activity is specific for levoglucosan and NAD+. Poor substrates: ribose and glucose
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.65
substrate 1,5-anhydro-D-glucitol, pH 8.5, 40°C
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.
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
-
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). F0M433_PSEPM
Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG 23796 / Sphe3)
390
0
42118
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.425)
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.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda5 Ver: 9edf756-main (2022-05-17 10:30:03 +0200)