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Information on EC 1.1.1.173 - L-rhamnose 1-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.173
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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
1.1.1.173 L-rhamnose 1-dehydrogenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.173
-
nonphosphorylated
- stipitis
- l-lactate
- l-lactaldehyde
-
entner-doudoroff
-
pichia
-
azotobacter
- vinelandii
- l-rhamnonate
- dehydratase
showSynonyms
l-rhamnose-1-dehydrogenase, l-rhamnose 1-dehydrogenase, sulth_3559, nad-utilizing l-rhamnose 1-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AN4186
L-rhamnose-1-dehydrogenase
LraA
NAD-utilizing L-rhamnose 1-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
-
-
-
-
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
the catalytic triad is formed by conserved Ser148-Tyr161-Lys165 residues
-
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
the catalytic triad is formed by conserved Ser-Tyr-Lys residues
-
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+
the catalytic triad is formed by conserved Ser-Tyr-Lys residues
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-rhamnose degradation II, L-rhamnose degradation III
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SYSTEMATIC NAME
IUBMB Comments
L-rhamnofuranose:NAD+ 1-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
52227-67-5
-
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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
L-rhamnose + NADP+
L-rhamno-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: pro-S (B) specific
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: product unstable, apparent product L-rhamnonate
Products: product unstable, apparent product L-rhamnonate
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: the enzyme is involved in the rhamnose metabolism, overview
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: the heterologous protein shows the highest activity and affinity with L-rhamnose and a lower activity and affinity with L-mannose and L-lyxose
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: the enzyme is involved in the rhamnose metabolism, overview
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: the heterologous protein shows the highest activity and affinity with L-rhamnose and a lower activity and affinity with L-mannose and L-lyxose
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: product unstable, apparent product L-rhamnonate
Products: product unstable, apparent product L-rhamnonate
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH + H+
A0A1U8QWV9
Substrates: -
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH + H+
A0A1U8QWV9
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates are: D-glucose, D-mannose, D-galactose, D-fructose, D-xylose, D-fucose, D-arabinose, D-lyxose, D-ribose, D-fucose, L-fucose, L-xylose, L-arabinose, L-sorbose, sorbitol, mannitol, xylitol, 2,3-butanediol, 2-dehydro-3-deoxy-L-rhamnonate, and L-rhamnonate
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
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: product unstable, apparent product L-rhamnonate
Products: product unstable, apparent product L-rhamnonate
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: the enzyme is involved in the rhamnose metabolism, overview
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: the enzyme is involved in the rhamnose metabolism, overview
Products: -
Products: -
r
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH
-
Substrates: -
Products: product unstable, apparent product L-rhamnonate
Products: product unstable, apparent product L-rhamnonate
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme transcription in Pichia stipitis is induced during growth on L-rhamnose but not on other carbon sources
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
substrate specificity, overview
-
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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
1.11
-
substrate L-rhamnose, cosubstrate NADP+, pH 9.5, 50°C
1.22
-
substrate L-mannose, cosubstrate NAD+, pH 9.5, 50°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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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
physiological function
physiological function
A0A1U8QWV9
deletion of Lra severely impairs L-rhamnose utilization and impairs the production of alpha-L-rhamnosidases
physiological function
-
deletion of Lra severely impairs L-rhamnose utilization and impairs the production of alpha-L-rhamnosidases
-
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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). RM1DH_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
258
0
27207
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 42.8fold by anion exchange chromatography, ultrafiltration, gel filtration, hydroxyapatite chromatography, and again gel filtration, recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant enzyme in analytical amounts from Saccharomyces cerevisiae by anion exchange chromatography, and native and SDS-PAGE, tagging of the enzyme strongly affects its activity, overview
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli
gene RHA1, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cereviaie
-
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli
-
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by L-rhamnose via RhaR
expression is repressed by D-glucose, repression is independently of CreA
expression is repressed by D-glucose, repression is independently of CreA
A0A1U8QWV9
expression is repressed by D-glucose, repression is independently of CreA
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mostad, S.B.; Helming, H.L.; Groom, C.; Glasfeld, A.
The stereospecificity of hydrogen transfer to NAD(P)+ catalyzed by lactol dehydrogenases
Biochem. Biophys. Res. Commun.
233
681-686
1997
Aureobasidium pullulans
brenda
Pittner, F.; Turecek, P.L.
The application of immobilized alpha-L-rhamnosidase and L-rhamnosedehydrogenase in the analysis of L-rhamnose and alpha-L-rhamnosides
Appl. Biochem. Biotechnol.
16
15-24
1987
Aureobasidium pullulans
-
brenda
Rigo, L.U.; Nakano, M.; Veiga, L.A.; Feingold, D.S.
L-Rhamnose dehydrogenase of pullularia pullulans
Biochim. Biophys. Acta
445
286-293
1976
Aureobasidium pullulans
brenda
Pardo, E.H.; Funayama, S.; Pedrosa, F.O.; Rigo, L.U.
Pichia stipitis L-rhamnose dehydrogenase and a catabolite-resistant mutant able to utilize 2-deoxy-D-glucose
Can. J. Microbiol.
38
417-422
1992
Scheffersomyces stipitis
-
brenda
Twerdochlib, A.L.; Pedrosa, F.O.; Funayama, S.; Rigo, L.U.
L-Rhamnose metabolism in Pichia stipitis and Debaryomyces polymorphus
Can. J. Microbiol.
40
896-902
1994
Scheffersomyces stipitis
-
brenda
Koivistoinen, O.M.; Hilditch, S.; Voutilainen, S.P.; Boer, H.; Penttilae, M.; Richard, P.
Identification in the yeast Pichia stipitis of the first L-rhamnose-1-dehydrogenase gene
FEBS J.
275
2482-2488
2008
Scheffersomyces stipitis, Scheffersomyces stipitis NRC 5568
brenda
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
Debaryomyces hansenii, Debaryomyces hansenii NBRC0083, Scheffersomyces stipitis
brenda
Bae, J.; Kim, S.M.; Lee, S.B.
Identification and characterization of 2-keto-3-deoxy-L-rhamnonate dehydrogenase belonging to the MDR superfamily from the thermoacidophilic bacterium Sulfobacillus thermosulfidooxidans: implications to L-rhamnose metabolism in archaea
Extremophiles
19
469-478
2015
Sulfobacillus thermosulfidooxidans
brenda
MacCabe, A.P.; Ninou, E.I.; Pardo, E.; Orejas, M.
Catabolism of L-rhamnose in A. nidulans proceeds via the non-phosphorylated pathway and is glucose repressed by a CreA-independent mechanism
Microb. Cell Fact.
19
188
2020
Aspergillus nidulans (A0A1U8QWV9), Aspergillus nidulans ATCC 38163 (A0A1U8QWV9)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.173)
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