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Literature summary for 1.1.1.376 extracted from

  • Johnsen, U.; Sutter, J.M.; Zaiß, H.; Schönheit, P.
    L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of L-arabinose dehydrogenase (2013), Extremophiles, 17, 897-909.
    View publication on PubMed
Search for more literature for 1.1.1.376

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Haloferax volcanii

Metals/Ions

Metals/Ions Comment Organism Structure
KCl activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl Haloferax volcanii
NaCl activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 4 * 28000, SDS-PAGE Haloferax volcanii
130000
-
 gel filtration Haloferax volcanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arabinose + NAD(P)+ Haloferax volcanii the enzyme initiates L-arabinose degradation L-arabinono-1,4-lactone + NAD(P)H + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GP33
-
-
Haloferax volcanii DSM 3757 D4GP33
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arabinose + NAD(P)+ the enzyme initiates L-arabinose degradation Haloferax volcanii L-arabinono-1,4-lactone + NAD(P)H + H+
-
 ?
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+
-
 ?
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+
-
 ?
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+
-
 ?
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+
-
 ?
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+
-
 ?
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+
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 28000, SDS-PAGE Haloferax volcanii

Synonyms

Synonyms Comment Organism
HVO_B0032 locus name Haloferax volcanii
L-AraDH
-
 Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Haloferax volcanii

pH Range

pH Minimum pH Maximum Comment Organism
6 10 50% of maximal activity is found at pH values of 6 and 10 Haloferax volcanii

Cofactor

Cofactor Comment Organism Structure
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
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

Expression

Organism Comment Expression
Haloferax volcanii transcriptionally induced by both L-arabinose and D-xylose up

General Information

General Information Comment Organism
malfunction the L-AraDH deletion mutant does not grow on L-arabinose, whereas growth on D-xylose and glucose is unaffected Haloferax volcanii
physiological function the enzyme is functionally involved in L-arabinose catabolism but not in D-xylose degradation Haloferax volcanii