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 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
25000 | - |
x * 25000, SDS-PAGE | Scheffersomyces stipitis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Debaryomyces hansenii | - |
gene LRA1 | - |
Debaryomyces hansenii NBRC0083 | - |
gene LRA1 | - |
Scheffersomyces stipitis | - |
gene LRA1 | - |
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 | 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 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 | 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 | Comment | Organism |
---|---|---|
? | x * 25000, SDS-PAGE | Scheffersomyces stipitis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
oxidation assay at | Debaryomyces hansenii |
30 | - |
oxidation assay at | Scheffersomyces stipitis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
oxidation assay at | Debaryomyces hansenii |
9 | - |
oxidation assay at | Scheffersomyces stipitis |
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 |