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Enzyme Nomenclature
Information on EC 4.2.1.90 - L-rhamnonate dehydratase
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EC Tree
4.2.1.90 L-rhamnonate dehydrataseSpecify your search results
Word Map
- 4.2.1.90
- stipitis
- vinelandii
-
azotobacter
-
pichia
- l-lactaldehyde
- niger
-
entner-doudoroff
-
nonphosphorylated
-
ladhs
- l-lactate
The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydratase, L-rhamnonate
-
-
-
-
LRA3
LraC
PICST_50672
RhamD
additional information
LraC
Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
-
-
additional information
the enyzme belongs to the enolase superfamily of enzymes
additional information
the enyzme belongs to the enolase superfamily of enzymes
additional information
the enyzme belongs to the enolase superfamily of enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O
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-
-
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L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O
reaction mechanism of the RhamD-catalyzed reaction, overview
L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O
reaction mechanism of the RhamD-catalyzed reaction, overview
L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O
reaction mechanism of the RhamD-catalyzed reaction, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage by elimination of water
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-rhamnonate hydro-lyase (2-dehydro-3-deoxy-L-rhamnonate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
99533-47-8
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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
L-lyxonate
? + H2O
-
-
-
?
L-lyxonate
? + H2O
best substrate, 128% activity compared to L-rhamnonate
-
-
?
L-lyxonate
? + H2O
-
best substrate, 128% activity compared to L-rhamnonate
-
-
?
L-mannonate
2-dehydro-3-deoxy-L-mannonate + H2O
Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
-
-
-
?
L-mannonate
? + H2O
-
-
-
?
L-mannonate
? + H2O
-
89.2% activity compared to L-rhamnonate
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
enzyme of an oxidative pathway in the degradation of L-rhamnose
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
the catalytic mechanism is similar to those of the known acid-sugar dehydratases in this protein family
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-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
the catalytic mechanism is similar to those of the known acid-sugar dehydratases in this protein family
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-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
i.e. 6-deoxy-L-mannonate
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
i.e. 6-deoxy-L-mannonate
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
i.e. 6-deoxy-L-mannonate
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
Scheffersomyces stipitis ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
a step in the rhamnose metabolic pathway, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
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a step in the rhamnose metabolic pathway, overview
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-
?
additional information
?
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the recombinant enzyme shows high activity with L-rhamnonate and L-mannonate
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additional information
?
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enzyme LraC shows activity with L-rhamnonate and L-mannonate. The production of 2-dehydro-3-deoxy sugar is measured with the thiobarbituric acid assay. Substrate specificity analysis, overview. No activity with L-galactonate, D-gulonate, D-gluconate, L-gulonate, D-arabonate, D-lyxonate, L-lyxonate, D-xylonate, mucic acid, L-fuconate, D-mannonate, D-riborate, L-arabonate, D-galactonate, D-galacturonate, and D-glucuronate
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additional information
?
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the recombinant enzyme shows high activity with L-rhamnonate and L-mannonate
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additional information
?
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Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
enzyme LraC shows activity with L-rhamnonate and L-mannonate. The production of 2-dehydro-3-deoxy sugar is measured with the thiobarbituric acid assay. Substrate specificity analysis, overview. No activity with L-galactonate, D-gulonate, D-gluconate, L-gulonate, D-arabonate, D-lyxonate, L-lyxonate, D-xylonate, mucic acid, L-fuconate, D-mannonate, D-riborate, L-arabonate, D-galactonate, D-galacturonate, and D-glucuronate
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additional information
?
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L-arabonate, D-gluconate, L-fuconate or D-galactonate at 0.002 or 0.02 M are no substrates
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-
additional information
?
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stereochemical course of the RhamD-catalyzed reaction, overview
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additional information
?
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stereochemical course of the RhamD-catalyzed reaction, overview
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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
L-lyxonate
? + H2O
best substrate, 128% activity compared to L-rhamnonate
-
-
?
L-lyxonate
? + H2O
-
best substrate, 128% activity compared to L-rhamnonate
-
-
?
L-mannonate
? + H2O
-
89.2% activity compared to L-rhamnonate
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
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enzyme of an oxidative pathway in the degradation of L-rhamnose
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
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-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
step in the alternative pathway for L-rhamnose metabolism, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
Scheffersomyces stipitis ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
-
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
a step in the rhamnose metabolic pathway, overview
-
-
?
L-rhamnonate
2-dehydro-3-deoxy-L-rhamnonate + H2O
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a step in the rhamnose metabolic pathway, overview
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
L-lyxonate
pH 7.9, 25°C, wild-type enzyme
0.06
L-mannonate
pH 7.9, 25°C, wild-type enzyme
0.25
L-Rhamnonate
pH 7.9, 25°C, wild-type enzyme
3
L-Rhamnonate
recombinant enzyme, pH 7.0, temperature not specified in the publication
additional information
additional information
the kcat/Km value with L-rhamnonate is 26.2fold and 59.2fold higher than those with L-lyxonate and L-mannonate, respectively, mainly due to 13.6fold and 30.2fold higher Km values, respectively
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additional information
additional information
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Michaelis-Menten kinetics, overview
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additional information
additional information
Michaelis-Menten kinetics, overview
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additional information
additional information
Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
L-lyxonate
pH 7.9, 25°C, wild-type enzyme
0.1
L-mannonate
pH 7.9, 25°C, wild-type enzyme
3.9
L-Rhamnonate
pH 7.9, 25°C, wild-type enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
-
UniProt
brenda
Aspergillus niger CBS 141257
the CBS 141257 strain is obtained by transformation of strain N593.20 with uridine (pyrG) from Aspergillus oryzae
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-
brenda
Scheffersomyces stipitis ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
i.e. Pichia stipitis
UniProt
brenda
the CBS 141257 strain is obtained by transformation of strain N593.20 with uridine (pyrG) from Aspergillus oryzae
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
-
a double deletion of lraC and lraA in Aspergillus niger results in a strain that exhibits no L-rhamnose dehydrogenase activity and cannot consume or grow on L-rhamnose. Deletion of the clustered genes lraA, lraB or lraC causes a reduction in expression level of the other genes of the L-rhamnose pathway, rhtA is not expressed in the DELTAlraC and DELATrhaR mutants. Strongly reduced expression levels of lraA, lraB, rhaR, rglB, rgxA and rgaeA are observed in the DELTAlraC mutant upon the 2 h transfer to L-rhamnonate compared to the reference strain
malfunction
Aspergillus niger CBS 141257
-
a double deletion of lraC and lraA in Aspergillus niger results in a strain that exhibits no L-rhamnose dehydrogenase activity and cannot consume or grow on L-rhamnose. Deletion of the clustered genes lraA, lraB or lraC causes a reduction in expression level of the other genes of the L-rhamnose pathway, rhtA is not expressed in the DELTAlraC and DELATrhaR mutants. Strongly reduced expression levels of lraA, lraB, rhaR, rglB, rgxA and rgaeA are observed in the DELTAlraC mutant upon the 2 h transfer to L-rhamnonate compared to the reference strain
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metabolism
the enzyme is involved in L-rhamnose catabolism. Eukaryotic L-rhamnose pathway, overview
metabolism
-
L-rhamnonate dehydratase (LraC) probably converts L-rhamnonate to 2-dehydro-3-deoxy-L-rhamnonate (L-KDR), catalyzing the third step of the non-phosphorylative pathway. The inducer of RhaR is beyond L-rhamnonate dehydratase (LraC) and is likely to be the 2-keto-3-L-deoxyrhamnonate
metabolism
L-rhamnonate dehydratase (LRA3) converts L-rhamnonate to 2-dehydro-3-deoxy-L-rhamnonate (L-KDR), catalyzing the third step of the non-phosphorylative pathway in Schefferomyces stipitis. The inducer of RhaR is beyond L-rhamnonate dehydratase (LraC) and is likely to be the 2-keto-3-L-deoxyrhamnonate
metabolism
L-rhamnose is oxidised to L-rhamnonate which is then reacting with a dehydratase. The resulting 3,6-dideoxy-L-erythro-hexulosonic acid (2-dehydro-3-deoxy rhamnonate) is subsequently split by and aldolase to pyruvate and L-lactaldehyde
metabolism
Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7
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L-rhamnose is oxidised to L-rhamnonate which is then reacting with a dehydratase. The resulting 3,6-dideoxy-L-erythro-hexulosonic acid (2-dehydro-3-deoxy rhamnonate) is subsequently split by and aldolase to pyruvate and L-lactaldehyde
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metabolism
Aspergillus niger CBS 141257
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L-rhamnonate dehydratase (LraC) probably converts L-rhamnonate to 2-dehydro-3-deoxy-L-rhamnonate (L-KDR), catalyzing the third step of the non-phosphorylative pathway. The inducer of RhaR is beyond L-rhamnonate dehydratase (LraC) and is likely to be the 2-keto-3-L-deoxyrhamnonate
-
metabolism
Scheffersomyces stipitis ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
-
L-rhamnonate dehydratase (LRA3) converts L-rhamnonate to 2-dehydro-3-deoxy-L-rhamnonate (L-KDR), catalyzing the third step of the non-phosphorylative pathway in Schefferomyces stipitis. The inducer of RhaR is beyond L-rhamnonate dehydratase (LraC) and is likely to be the 2-keto-3-L-deoxyrhamnonate
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Show AA Sequence and Transmembrane Helices (1615 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
RhamD crystallizes as an octamer, in agreement with the oligomeric structure determined by gel filtration
additional information
RhamD crystallizes as an octamer, in agreement with the oligomeric structure determined by gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
RhamD contains an N-terminal alpha+beta capping domain and a C-terminal (beta/alpha)7beta-barrel, i.e. a modified TIM-barrel, catalytic domain with the active site located at the interface between the two domains
additional information
additional information
RhamD contains an N-terminal alpha+beta capping domain and a C-terminal (beta/alpha)7beta-barrel, i.e. a modified TIM-barrel, catalytic domain with the active site located at the interface between the two domains
additional information
-
RhamD contains an N-terminal alpha+beta capping domain and a C-terminal (beta/alpha)7beta-barrel, i.e. a modified TIM-barrel, catalytic domain with the active site located at the interface between the two domains
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to Mg2+, the protein solution contains 42 mg/mL RhamD in 10 mM HEPES, pH 7.5, 150 mM NaCl, 10 mM L-methionine, and 10% glycerol, the precipitant solution contains 1.2 M ammonium sulfate, 100 mM Tris-HCl, pH 8.5, and 0.2 M lithium sulfate, 2 days, X-ray diffraction structure determination and analysis at 2.1 A resolution, RhamD crystallizes as an octamer
enzyme bound to Mg2+ and 3-deoxy-L-rhamnonate, hanging drop method at room temperature, the protein solution for the Mg2+-enzyme complex contains 9.7 mg/mL RhamD in 10 mM HEPES, pH 7.5, containing 150 mM NaCl, 10 mM L-methionine, 5 mM DTT, 10% glycerol, and 5 mM MgCl2, the precipitant solution contains 2.4 M sodium malonate, pH 7.0, and 5 mM MgCl2, for the tertiary complex the protein solution contains 42 mg/mL RhamD in 10 mM in HEPES, pH 7.5, 150 mm NaCl, 10 mM L-methionine, 5 mM DTT, 10% glycerol, 5 mM MgCl2, and 40 mM 3-deoxy-L-rhamnonate, the precipitant solution contains 60% Tacsimate, pH 7.0, and 5 mM MgCl2, 3-4 days, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution, RhamD crystallizes as an octamer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H281N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H329N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
additional information
-
construction of a DELTAlraC knockout mutant from strain CBS 141257, gene deletion and transcriptomic analysis is performed to elucidate the function of LraC, protoplast-mediated transformations of Aspergillus niger. Deletion of genes lraA, lraB or lraC causes a reduction in expression level of the other genes of the L-rhamnose pathway. Strongly reduced expression levels of lraA, lraB, rhaR, rglB, rgxA and rgaeA are observed in the DELTAlraC mutant upon the 2 h transfer to L-rhamnonate compared to the reference strain. But none of the deletions of genes lraA, lraB or lraC results in accumulation of the inducer of the pathway regulator (RhaR)
additional information
Aspergillus niger CBS 141257
-
construction of a DELTAlraC knockout mutant from strain CBS 141257, gene deletion and transcriptomic analysis is performed to elucidate the function of LraC, protoplast-mediated transformations of Aspergillus niger. Deletion of genes lraA, lraB or lraC causes a reduction in expression level of the other genes of the L-rhamnose pathway. Strongly reduced expression levels of lraA, lraB, rhaR, rglB, rgxA and rgaeA are observed in the DELTAlraC mutant upon the 2 h transfer to L-rhamnonate compared to the reference strain. But none of the deletions of genes lraA, lraB or lraC results in accumulation of the inducer of the pathway regulator (RhaR)
-
additional information
introduction of genes LRA1-4 or LRA1-3, LRA5 and LAR6 compensats for the L-rhamnose-defective phenotype of an Escherichia coli mutant
additional information
-
introduction of genes LRA1-4 or LRA1-3, LRA5 and LAR6 compensats for the L-rhamnose-defective phenotype of an Escherichia coli mutant
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NRC 5568, PR1 mutant, partial; strain 1747, partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene LRA3, genetic organization, L-rhamnose catabolism genes RHA1, LRA2, LRA3 and LRA4 are organized in a chromosomal gene cluster in Scheffersomyces stipitis. In Scheffersomyces stipitis, another transcription factor than TRC1 is found in the L-rhamnose cluster, FST14. This transcription factor is more up-regulated than TRC1 on L-rhamnose and it might be co-regulating the pectinolytic genes together with TRC1
gene lraC, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae
gene lraC, DNA and amino acid sequencedetermination and analysis, expression in Saccharomyces cerevisiae
-
gene lraC, genetic organization, genes lraA, lraB and lraC, as well as the L-rhamnose regulator RhaR are organized in a cluster
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gene yfaW, expression of the His6- or His10-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
the genes for L-rhamnose catabolism RHA1, LRA2, LRA3 and LRA4 but not LADH are clustered, genetic organization, phylogenetic analysis, overview. Functional expression of gene LRA3 in Saccharomyces cerevisiae with a strong constitutive promoter. C-terminally his-tagged protein shows no activity and the activity of the N-terminally tagged protein is reduced by about 95%, so the enzyme is expressed without tagand not purified
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Schwanniomyces polymorphus, Schwanniomyces polymorphus 1747
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brenda
Rigo, L.U.; Marechal, L.R.; Vieira, M.M.; Veiga, L.A.
Oxidative pathway for L-rhamnose degradation in Pullularia pullulans
Can. J. Microbiol.
31
817-822
1985
Aureobasidium pullulans
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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
Azotobacter vinelandii, Azotobacter vinelandii NBRC 102612, Debaryomyces hansenii, Debaryomyces hansenii NBRC0083, Scheffersomyces stipitis
brenda
Rakus, J.F.; Fedorov, A.A.; Fedorov, E.V.; Glasner, M.E.; Hubbard, B.K.; Delli, J.D.; Babbitt, P.C.; Almo, S.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase
Biochemistry
47
9944-9954
2008
Escherichia coli K-12, Escherichia coli K-12 (P77215), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZNF9), Salmonella enterica subsp. enterica serovar Typhimurium LT2 (Q8ZNF9)
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
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Sphingomonas sp. (Q1NEI8), Sphingomonas sp.
brenda
Motter, F.A.; Kuivanen, J.; Keraenen, H.; Hilditch, S.; Penttilae, M.; Richard, P.
Categorisation of sugar acid dehydratases in Aspergillus niger
Fungal Genet. Biol.
64
67-72
2014
Aspergillus niger, Aspergillus niger ATCC 1015
brenda
Koivistoinen, O.M.; Arvas, M.; Headman, J.R.; Andberg, M.; Penttilae, M.; Jeffries, T.W.; Richard, P.
Characterisation of the gene cluster for L-rhamnose catabolism in the yeast Scheffersomyces (Pichia) stipitis
Gene
492
177-185
2012
Scheffersomyces stipitis (A3LZU6)
brenda
Khosravi, C.; Kun, R.S.; Visser, J.; Aguilar-Pontes, M.V.; de Vries, R.P.; Battaglia, E.
In vivo functional analysis of L-rhamnose metabolic pathway in Aspergillus niger a tool to identify the potential inducer of RhaR
BMC Microbiol.
17
214-227
2017
Aspergillus niger, Aspergillus niger CBS 141257, Scheffersomyces stipitis (A3LZU6), Scheffersomyces stipitis ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545 (A3LZU6)
brenda
Motter, F.A.; Kuivanen, J.; Keraenen, H.; Hilditch, S.; Penttilae, M.; Richard, P.
Categorisation of sugar acid dehydratases in Aspergillus niger
Fungal Genet. Biol.
64
67-72
2014
Aspergillus niger, Aspergillus niger (G3XPU3), Aspergillus niger ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7 (G3XPU3)
brenda
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