Any feedback?
No. of entries
Information on EC 1.1.1.378 - L-rhamnose 1-dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.378
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
1.1.1.378 L-rhamnose 1-dehydrogenase [NAD(P)+]
IUBMB Comments
The enzyme, which occurs in the bacteria Azotobacter vinelandii and Sphingomonas sp. SKA58, is part of the non-phosphorylative degradation pathway for L-rhamnose. The enzyme differs in cofactor specificity from EC 1.1.1.173, L-rhamnose 1-dehydrogenase, which is specific for NAD+ and EC 1.1.1.377, L-rhamnose 1-dehydrogenase (NADP+).
The enzyme appears in viruses and cellular organisms
showSynonyms
rhadh, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EAT09360
LRA1
SpLRA1
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
L-rhamnose + NAD(P)+ = L-rhamnono-1,4-lactone + NAD(P)H + H+
-
-
-
-
L-rhamnose + NAD(P)+ = L-rhamnono-1,4-lactone + NAD(P)H + H+
in putative catalytic mechanism, the C1-OH group of L-rhamnose is deprotonated by Tyr159 as a general basic catalyst, with concurrent transfer of the hydride ion to NAD(P)+, and the pKa value of its hydroxyl group is lowered by Lysl63, leading to the stabilization of the tyrosinate anion at physiological pH
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-rhamnose degradation II, L-rhamnose degradation III
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-rhamnose:NAD(P)+ 1-oxidoreductase
The enzyme, which occurs in the bacteria Azotobacter vinelandii and Sphingomonas sp. SKA58, is part of the non-phosphorylative degradation pathway for L-rhamnose. The enzyme differs in cofactor specificity from EC 1.1.1.173, L-rhamnose 1-dehydrogenase, which is specific for NAD+ and EC 1.1.1.377, L-rhamnose 1-dehydrogenase (NADP+).
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-fucose + NAD+
?
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
L-fucose + NADP+
?
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
L-lyxose + NAD+
?
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
L-mannose + NAD+
?
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
L-rhamnose + NAD(P)+
L-rhamno-1,4-lactone + NAD(P)H + H+
-
Substrates: first enzyme of the non-phosphorylative L-rhamnose pathway in archaea, that is analogous to the Entner-Doudoroff pathway
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH + H+
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
L-rhamnose + NADP+
L-rhamno-1,4-lactone + NADPH + H+
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: the C5-OH and C6-methyl groups of L-rhamnose are recognized by specific residues of RhaDH through hydrogen bonds and hydrophobic contact, respectively, which contribute to the different substrate specificities from other aldose 1-dehydrogenases in the short-chain dehydrogenase/reductase superfamily
Products: -
Products: -
-
L-lyxose + NADP+
?
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
L-lyxose + NADP+
?
-
Substrates: activity is 75% compared to the activity with L-rhamnose and NADP+
Products: -
Products: -
?
L-lyxose + NADP+
?
-
Substrates: activity is 75% compared to the activity with L-rhamnose and NADP+
Products: -
Products: -
?
L-mannose + NADP+
?
-
Substrates: the enzyme shows significant preference for NADP+ over NAD+
Products: -
Products: -
?
L-mannose + NADP+
?
-
Substrates: activity is 8.4% compared to the activity with L-rhamnose and NADP+
Products: -
Products: -
?
L-mannose + NADP+
?
-
Substrates: activity is 8.4% compared to the activity with L-rhamnose and NADP+
Products: -
Products: -
?
L-rhamnose + NAD(P)+
L-rhamnono-1,4-lactone + NAD(P)H + H+
-
Substrates: the enzyme is part of an alternative pathway of L-rhamnose metabolism by which L-rhamnose is converted into pyruvate and L-lactaldehyde, through reaction steps analogous to the Entner-Doudoroff pathway
Products: -
Products: -
?
L-rhamnose + NAD(P)+
L-rhamnono-1,4-lactone + NAD(P)H + H+
-
Substrates: the enzyme is part of an alternative pathway of L-rhamnose metabolism by which L-rhamnose is converted into pyruvate and L-lactaldehyde, through reaction steps analogous to the Entner-Doudoroff pathway
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamnono-1,4-lactone + NADH + H+
-
Substrates: L-rhamnose is the best substrate, preference for NADP+ over NAD+
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamnono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamnono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-rhamnose + NADP+
L-rhamnono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-rhamnose + NADP+
L-rhamnono-1,4-lactone + NADPH + H+
-
Substrates: L-rhamnose is the best substrate, preference for NADP+ over NAD+
Products: -
Products: -
?
L-rhamnose + NADP+
L-rhamnono-1,4-lactone + NADPH + H+
-
Substrates: -
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-rhamnose + NAD(P)+
L-rhamno-1,4-lactone + NAD(P)H + H+
-
Substrates: first enzyme of the non-phosphorylative L-rhamnose pathway in archaea, that is analogous to the Entner-Doudoroff pathway
Products: -
Products: -
?
L-rhamnose + NADP+
L-rhamnono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-rhamnose + NAD(P)+
L-rhamnono-1,4-lactone + NAD(P)H + H+
-
Substrates: the enzyme is part of an alternative pathway of L-rhamnose metabolism by which L-rhamnose is converted into pyruvate and L-lactaldehyde, through reaction steps analogous to the Entner-Doudoroff pathway
Products: -
Products: -
?
L-rhamnose + NAD(P)+
L-rhamnono-1,4-lactone + NAD(P)H + H+
-
Substrates: the enzyme is part of an alternative pathway of L-rhamnose metabolism by which L-rhamnose is converted into pyruvate and L-lactaldehyde, through reaction steps analogous to the Entner-Doudoroff pathway
Products: -
Products: -
?
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
-
significant interactions with the 2'-phosphate group of NADP+, but not the 2'-hydroxyl group of NAD+, are consistent with a significant preference for NADP+ over NAD+. Structural insights into coenzyme specificity, 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
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.
kcat/KM VALUE [1/mMs-1]
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
0.62
-
25°C, pH not specified in the publication, cell-free extract, NADP+-dependent activity
31.7
-
25°C, pH not specified in the publication, purified enzyme, NAD+-dependent activity
39.8
-
25°C, pH not specified in the publication, purified enzyme, NADP+-dependent activity
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
30
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
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 short-chain dehydrogenase/reductase superfamily
physiological function
additional information
-
structure-function analysis, overview. The side chains of Ser146 and Tyr159, Ser148 and Gln156, Thr191, and Asn197 and one water molecular (Wat23) form hydrogen bonds with the hydroxyl groups of C1, C2, C3, and C4 of L-rhamnose, respectively. Wat23 also interacts with the side chains of Asp200, and Lys163 formed hydrogen bond network with the main chains of Ala94 and Asn117 via one water molecular (Wat41). Among these residues, Ser146-Tyr159-Lys163, corresponding to a motif of the catalytic triad, and Ala94 and Asn117 are completely conserved in SDR superfamily enzymes. Phe99 appears to be more important for enzyme catalysis than Ile196
physiological function
-
first enzyme of the non-phosphorylative L-rhamnose pathway in archaea, that is analogous to the Entner-Doudoroff pathway
physiological function
-
several microorganisms can utilize L-rhamnose as a carbon and energy source through the non-phosphorylative metabolic pathway, in which L-rhamnose 1-dehydrogenase (RhaDH) catalyzes the NAD(P)+-dependent oxidization of Lrhamnose to L-rhamnono-1,4-lactone
physiological function
-
first enzyme of the non-phosphorylative L-rhamnose pathway in archaea, that is analogous to the Entner-Doudoroff pathway
-
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). A0A7W8T8Q7_9BURK
260
0
27144
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
additional information
-
the subunit of AvRhaDH was a single-domain protein with an alpha/beta doubly wound structure. A seven-stranded parallel beta-sheet (beta3-beta2-beta1-beta4-beta5-beta6-beta7) in the center of the molecule is sandwiched by two arrays of parallel alpha-helices (alpha1 to alpha6), which is a typical dinucleotide binding the Rossmann fold motif including the characteristic sequence Gly-X3-Gly-X-Gly; Gly12-Ala13-Ser14-Arg15-Gly16-Ile17-Gly18. Furthermore, a motif corresponding to Asn92-Asn93-Ala94-Gly95 is previously shown to be important for stabilizing this central beta-sheet in other SDR superfamily enzymes. A small domain containing the alpha7 and two 310 helixes is slightly separated from the main body of the subunit, and contained the flexible region
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in ligand-free, NAD+-bound, NADP+-bound, and L-rhamnose- and NAD+-bound forms, sitting drop vapor diffusion method, mixing of 500 nl of 10 mg/ml protein in 20 mM Tris/HCl, pH 8.0, and 150 mM NaCl, with 500 nl of reservoir olution containing 100 mM Tris/HCl, pH 8.5, 200 mM Li2SO4, and 25% w/v PEG 3350, with or without coenzyme, for the apoenzyme and for the NADP+-bound form,, and 100 mM Tris/HCl, pH 8.0, 200 mM NaCl, 24.5% w/v PEG 3350, and 3% v/v glycerol only for the NAD+-/L-rhamnose-bound form, equilibration against 0.07 ml of reservoir solution, at 20°C, X-ray diffraction structure determination and analysis at 1.9, 2.1, 2.4, and 1.6 A resolution, respectively, molecular replacement using the structure of 3-oxoacyl-(acyl carrier protein) reductase from Bacillus anthracis (PDB ID 2UVD) as the search model, modeling
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D200A
-
site-directed mutagenesis, the mutant shows 16% activity with L-rhamnose compared to wild-type
D200H
-
site-directed mutagenesis, the mutant shows 22% activity with L-rhamnose compared to wild-type
R15T
-
site-directed mutagenesis, the mutant of AvRhaDH shows a Km value for NADP+ decreased by 116fold, which increases the ratio of NADP+ to NAD+ (0.188) 157fold, from that of the wild-type enzyme (18.5)
S37H
-
site-directed mutagenesis, the mutant shows an altered ratio of NADP+ to NAD+ (0.101) compared to that of the wild-type enzyme (18.5)
T191F
-
site-directed mutagenesis, the mutant shows 3.9% activity with L-rhamnose compared to wild-type
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
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
Watanabe, S.; Saimura, M.; Makino, K.
Eukaryotic and bacterial gene clusters related to an alternative pathway of non-phosphorylated L-rhamnose metabolism
J. Biol. Chem.
283
20372-20382
2008
Azotobacter vinelandii, Azotobacter vinelandii NBRC 102612
brenda
Watanabe, S.; Makino, K.
Novel modified version of nonphosphorylated sugar metabolism-an alternative L-rhamnose pathway of Sphingomonas sp
FEBS J.
276
1554-1567
2009
Sphingomonas sp., Sphingomonas sp. NBRC 101715
brenda
Yoshiwara, K.; Watanabe, S.; Watanabe, Y.
Crystal structure of L-rhamnose 1-dehydrogenase involved in the nonphosphorylative pathway of L-rhamnose metabolism in bacteria
FEBS Lett.
595
637-646
2021
Azotobacter vinelandii
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.378)
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 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
