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Literature summary for 3.1.1.68 extracted from

  • Saha, S.; Hashino, M.; Suzuki, J.; Uda, A.; Watanabe, K.; Shimizu, T.; Watarai, M.
    Contribution of methionine sulfoxide reductase B (MsrB) to Francisella tularensis infection in mice (2017), FEMS Microbiol. Lett., 364, fnw260.
    View publication on PubMed
Search for more literature for 3.1.1.68

Cloned(Commentary)

Cloned (Comment) Organism
gene xacC, recombinant overexpression of His-tagged enzyme in Haloferax volcanii strain H1209, subcloning in Escherichia coli strain XL1-Blue MRF' Haloferax volcanii

Protein Variants

Protein Variants Comment Organism
additional information generation of a xacC deletion mutant, growth of DELTAxacC on 25 mM D-xylose and L-arabinose is compared to Haloferx volcanii wild-type strain H26, the wild type grows on L-arabinose, the xacC mutant shows a lower growth rate and a lower final optical density. The wild-type phenotype is recovered by in trans complementation of DELTAxacC with xacC. But growth of DELTAxacC on D-xylose is not significantly affected Haloferax volcanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0109
-
 D-xylono-1,4-lactone pH 7.5, 42°C, recombinant enzyme Haloferax volcanii
0.0371
-
 L-arabinono-1,4-lactone pH 7.5, 42°C, recombinant enzyme Haloferax volcanii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ best activating divalent cation, 150% activity compared to Mg2+ Haloferax volcanii
Fe2+ 21% activity compared to Mg2+ Haloferax volcanii
K+ highest activity at about 1 M KCl Haloferax volcanii
Mg2+ activates, Km is 0.2 mM Haloferax volcanii
Mn2+ 86% activity compared to Mg2+ Haloferax volcanii
additional information the enzyme requires divalent cations for activity Haloferax volcanii
Ni2+ 21% activity compared to Mg2+ Haloferax volcanii
Zn2+ 14% activity compared to Mg2+ Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 recombinant His-tagged enzyme, gel filtration Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GP31
-
-
Haloferax volcanii ATCC 29605 D4GP31
-
-
Haloferax volcanii DS2 D4GP31
-
-
Haloferax volcanii DSM 3757 D4GP31
-
-
Haloferax volcanii JCM 8879 D4GP31
-
-
Haloferax volcanii NBRC 14742 D4GP31
-
-
Haloferax volcanii NCIMB 2012 D4GP31
-
-
Haloferax volcanii VKM B-1768 D4GP31
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Haloferax volcanii strain H1209 by nickel affinity chromatography and gel filtration to homogeneity Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii D-xylonate
-
 ?
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii NCIMB 2012 D-xylonate
-
 ?
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii JCM 8879 D-xylonate
-
 ?
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii DS2 D-xylonate
-
 ?
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii DSM 3757 D-xylonate
-
 ?
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii ATCC 29605 D-xylonate
-
 ?
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii NBRC 14742 D-xylonate
-
 ?
D-xylono-1,4-lactone + H2O preferred substrate Haloferax volcanii VKM B-1768 D-xylonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii L-arabinonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii NCIMB 2012 L-arabinonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii JCM 8879 L-arabinonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii DS2 L-arabinonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii DSM 3757 L-arabinonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii ATCC 29605 L-arabinonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii NBRC 14742 L-arabinonate
-
 ?
L-arabinono-1,4-lactone + H2O about 50% activity compared to D-xylono-1,4-lactone Haloferax volcanii VKM B-1768 L-arabinonate
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii ?
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii NCIMB 2012 ?
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii JCM 8879 ?
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii DS2 ?
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii DSM 3757 ?
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii ATCC 29605 ?
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii NBRC 14742 ?
-
 ?
additional information enzyme XacC catalyzes the hydrolysis of both L-arabino-gamma -lactone and D-xylono-gamma -lactone to the corresponding acids characterizing XacC as pentonolactonase. Additional small amounts of arabinonate and D-xylonate are likely formed by spontaneous hydrolysis Haloferax volcanii VKM B-1768 ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 31400, about, sequence calculation, 1 * 35000, recombinant His-tagged enzyme, SDS-PAGE Haloferax volcanii

Synonyms

Synonyms Comment Organism
D-xylonolactonase
-
 Haloferax volcanii
HVO_B0030
-
 Haloferax volcanii
lactonase
-
 Haloferax volcanii
More cf. EC 3.1.1.15 Haloferax volcanii
pentonolactonase
-
 Haloferax volcanii
XacC
-
 Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
 assay at Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Haloferax volcanii

Expression

Organism Comment Expression
Haloferax volcanii gene xacC is transcriptionally induced by both L-arabinose and D-xylose, and the regulator XacR up

General Information

General Information Comment Organism
metabolism the enzyme is possibly involved in the oxidative pathway of L-arabinose degradation to 2-oxoglutarate, a functional lactonase in sugar catabolism. Functional involvement of XacC in L-arabinose and D-xylose degradation Haloferax volcanii
physiological function functional involvement of the pentolactonase in pentose degradation. Gene xacC of the pentose degradation pathway is transcriptionally activated by the regulator XacR, as well as L-arabinose and D-xylose Haloferax volcanii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10.74
-
 L-arabinono-1,4-lactone pH 7.5, 42°C, recombinant enzyme Haloferax volcanii
20.96
-
 D-xylono-1,4-lactone pH 7.5, 42°C, recombinant enzyme Haloferax volcanii