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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: Bacteria, Eukaryota, Archaea
- 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 Ser-Tyr-Lys residues
-
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
-
-
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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: -
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: 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+
Substrates: -
Products: -
Products: -
?
L-rhamnose + NAD+
L-rhamno-1,4-lactone + NADH + H+
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: -
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: 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
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
other Location (Reliability: 3)
D4GPB7_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
265
0
27976
TrEMBL
-
A0A0P0REG4_9BURK
260
0
27131
TrEMBL
-
A0A6J4VMT1_9CHLR
251
0
25911
TrEMBL
-
E1VAZ8_HALED
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
256
0
26668
TrEMBL
-
A0A160TH27_9ZZZZ
253
0
26114
TrEMBL
other Location (Reliability: 3)
A0A2P6S6J9_ROSCH
322
1
35900
TrEMBL
other Location (Reliability: 3)
A0A7L8XEC2_EMEND
271
0
28656
TrEMBL
other Location (Reliability: 3)
A0A7W8T8Q7_9BURK
260
0
27144
TrEMBL
-
A0A1U8QWV9_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
267
0
28298
TrEMBL
-
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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
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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