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Literature summary for 1.1.1.173 extracted from

  • Watanabe, S.; Saimura, M.; Makino, K.
    Eukaryotic and bacterial gene clusters related to an alternative pathway of non-phosphorylated L-rhamnose metabolism (2008), J. Biol. Chem., 283, 20372-20382.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli Debaryomyces hansenii
gene LRA1, DNA and amino acid sequence determination and analysis, genetic organization, functional expression of His-tagged enzyme in Escherichia coli Scheffersomyces stipitis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.71
-
L-rhamnose pH 9.0, 30°C, recombinant enzyme Scheffersomyces stipitis
9.35
-
L-rhamnose pH 9.0, 30°C, recombinant enzyme Debaryomyces hansenii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
x * 25000, SDS-PAGE Scheffersomyces stipitis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-rhamnose + NAD+ Debaryomyces hansenii
-
L-rhamno-1,4-lactone + NADH
-
r
L-rhamnose + NAD+ Scheffersomyces stipitis
-
L-rhamno-1,4-lactone + NADH
-
r
L-rhamnose + NAD+ Debaryomyces hansenii NBRC0083
-
L-rhamno-1,4-lactone + NADH
-
r

Organism

Organism UniProt Comment Textmining
Debaryomyces hansenii
-
gene LRA1
-
Debaryomyces hansenii NBRC0083
-
gene LRA1
-
Scheffersomyces stipitis
-
gene LRA1
-

Purification (Commentary)

Purification (Comment) Organism
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 Scheffersomyces stipitis
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Debaryomyces hansenii

Reaction

Reaction Comment Organism Reaction ID
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+ the catalytic triad is formed by conserved Ser-Tyr-Lys residues Debaryomyces hansenii
L-rhamnofuranose + NAD+ = L-rhamno-1,4-lactone + NADH + H+ the catalytic triad is formed by conserved Ser148-Tyr161-Lys165 residues Scheffersomyces stipitis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
29.9
-
purified native enzyme Scheffersomyces stipitis
50.4
-
purified recombinant enzyme Scheffersomyces stipitis
53.3
-
purified recombinant enzyme Debaryomyces hansenii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-rhamnose + NAD+
-
Debaryomyces hansenii L-rhamno-1,4-lactone + NADH
-
r
L-rhamnose + NAD+
-
Scheffersomyces stipitis L-rhamno-1,4-lactone + NADH
-
r
L-rhamnose + NAD+
-
Debaryomyces hansenii NBRC0083 L-rhamno-1,4-lactone + NADH
-
r

Subunits

Subunits Comment Organism
? x * 25000, SDS-PAGE Scheffersomyces stipitis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
oxidation assay at Debaryomyces hansenii
30
-
oxidation assay at Scheffersomyces stipitis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1510
-
L-rhamnose pH 9.0, 30°C, recombinant enzyme Scheffersomyces stipitis
2860
-
L-rhamnose pH 9.0, 30°C, recombinant enzyme Debaryomyces hansenii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
oxidation assay at Debaryomyces hansenii
9
-
oxidation assay at Scheffersomyces stipitis

Cofactor

Cofactor Comment Organism Structure
NAD+ strictly dependent on Debaryomyces hansenii
NAD+ strictly dependent on Scheffersomyces stipitis
NADH strictly dependent on Debaryomyces hansenii
NADH strictly dependent on Scheffersomyces stipitis