EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.46 | expressed in Escherichia coli Rosetta (DE3)-pLysS cells | Haloferax volcanii |
1.1.1.376 | expression in Escherichia coli | Haloferax volcanii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.46 | 2 | - |
NAD+ | at pH 8.5 and 45°C | Haloferax volcanii | |
1.1.1.46 | 2.1 | - |
NADP+ | at pH 8.5 and 45°C | Haloferax volcanii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.46 | K+ | dependent on with with maximal activity at 1.5 M | Haloferax volcanii | |
1.1.1.46 | Na+ | dependent on with with maximal activity at 1.0 M | Haloferax volcanii | |
1.1.1.376 | KCl | activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl | Haloferax volcanii | |
1.1.1.376 | NaCl | activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl | Haloferax volcanii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.46 | 27800 | - |
- |
Haloferax volcanii |
1.1.1.46 | 28000 | - |
2 * 28000, SDS-PAGE | Haloferax volcanii |
1.1.1.46 | 130000 | - |
gel filtration | Haloferax volcanii |
1.1.1.376 | 28000 | - |
4 * 28000, SDS-PAGE | Haloferax volcanii |
1.1.1.376 | 130000 | - |
gel filtration | Haloferax volcanii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.46 | L-arabinose + NAD+ | Haloferax volcanii | - |
L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NAD+ | Haloferax volcanii H26 | - |
L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NAD+ | Haloferax volcanii DSM 3757 | - |
L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NADP+ | Haloferax volcanii | - |
L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NADP+ | Haloferax volcanii H26 | - |
L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NADP+ | Haloferax volcanii DSM 3757 | - |
L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NAD(P)+ | Haloferax volcanii | the enzyme initiates L-arabinose degradation | L-arabinono-1,4-lactone + NAD(P)H + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.46 | Haloferax volcanii | D4GP33 | - |
- |
1.1.1.46 | Haloferax volcanii H26 | D4GP33 | - |
- |
1.1.1.376 | Haloferax volcanii | D4GP33 | - |
- |
1.1.1.376 | Haloferax volcanii DSM 3757 | D4GP33 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.46 | Sepharose CL 4B column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration | Haloferax volcanii |
1.1.1.376 | - |
Haloferax volcanii |
EC Number | Renatured (Comment) | Organism |
---|---|---|
1.1.1.46 | refolding buffer contains 3 M KCl, L-arabinose, NADP+ and glutathione | Haloferax volcanii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.46 | L-arabinose + NAD+ | - |
Haloferax volcanii | L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NAD+ | - |
Haloferax volcanii H26 | L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NAD+ | - |
Haloferax volcanii DSM 3757 | L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NADP+ | - |
Haloferax volcanii | L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NADP+ | - |
Haloferax volcanii H26 | L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.46 | L-arabinose + NADP+ | - |
Haloferax volcanii DSM 3757 | L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.46 | additional information | no activity with ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose | Haloferax volcanii | ? | - |
? | |
1.1.1.46 | additional information | no activity with ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose | Haloferax volcanii H26 | ? | - |
? | |
1.1.1.46 | additional information | no activity with ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose | Haloferax volcanii DSM 3757 | ? | - |
? | |
1.1.1.376 | L-arabinose + NAD(P)+ | the enzyme initiates L-arabinose degradation | Haloferax volcanii | L-arabinono-1,4-lactone + NAD(P)H + H+ | - |
? | |
1.1.1.376 | L-arabinose + NAD+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors | Haloferax volcanii | L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NAD+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors | Haloferax volcanii H26 | L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NAD+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors | Haloferax volcanii DSM 3757 | L-arabinono-1,4-lactone + NADH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NADP+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors | Haloferax volcanii | L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NADP+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors | Haloferax volcanii H26 | L-arabinono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NADP+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors | Haloferax volcanii DSM 3757 | L-arabinono-1,4-lactone + NADPH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.46 | homotetramer | 2 * 28000, SDS-PAGE | Haloferax volcanii |
1.1.1.46 | homotetramer | 2 * 27800, calculated from amino acid sequence | Haloferax volcanii |
1.1.1.376 | homotetramer | 4 * 28000, SDS-PAGE | Haloferax volcanii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.46 | L-arabinose dehydrogenase | - |
Haloferax volcanii |
1.1.1.46 | L-AraDH | - |
Haloferax volcanii |
1.1.1.376 | HVO_B0032 | locus name | Haloferax volcanii |
1.1.1.376 | L-AraDH | - |
Haloferax volcanii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.46 | 45 | - |
- |
Haloferax volcanii |
1.1.1.376 | 45 | - |
- |
Haloferax volcanii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.46 | 8.5 | - |
- |
Haloferax volcanii |
1.1.1.376 | 8.5 | - |
- |
Haloferax volcanii |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.46 | 6 | 10 | 50% activity at pH 6.0 and 10.0 | Haloferax volcanii |
1.1.1.376 | 6 | 10 | 50% of maximal activity is found at pH values of 6 and 10 | Haloferax volcanii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.46 | NAD+ | the enzyme shows slight preference for NADP+ over NAD+ | Haloferax volcanii | |
1.1.1.46 | NADP+ | the enzyme shows slight preference for NADP+ over NAD+ | Haloferax volcanii | |
1.1.1.376 | NAD+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+ | Haloferax volcanii | |
1.1.1.376 | NADP+ | the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+ | Haloferax volcanii |
EC Number | Organism | Comment | Expression |
---|---|---|---|
1.1.1.376 | Haloferax volcanii | transcriptionally induced by both L-arabinose and D-xylose | up |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.46 | metabolism | the enzyme is functionally involved in L-arabinose catabolism but not in D-xylose degradation | Haloferax volcanii |
1.1.1.376 | malfunction | the L-AraDH deletion mutant does not grow on L-arabinose, whereas growth on D-xylose and glucose is unaffected | Haloferax volcanii |
1.1.1.376 | physiological function | the enzyme is functionally involved in L-arabinose catabolism but not in D-xylose degradation | Haloferax volcanii |