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Literature summary extracted from
- Contribution of methionine sulfoxide reductase B (MsrB) to Francisella tularensis infection in mice (2017), FEMS Microbiol. Lett., 364, fnw260.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.68 | 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.1.68 | 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]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.68 | 0.0109 | - |
D-xylono-1,4-lactone | pH 7.5, 42°C, recombinant enzyme | Haloferax volcanii |  |
| 3.1.1.68 | 0.0371 | - |
L-arabinono-1,4-lactone | pH 7.5, 42°C, recombinant enzyme | Haloferax volcanii | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.68 | Co2+ | best activating divalent cation, 150% activity compared to Mg2+ | Haloferax volcanii | |
| 3.1.1.68 | Fe2+ | 21% activity compared to Mg2+ | Haloferax volcanii | |
| 3.1.1.68 | K+ | highest activity at about 1 M KCl | Haloferax volcanii | |
| 3.1.1.68 | Mg2+ | activates, Km is 0.2 mM | Haloferax volcanii | |
| 3.1.1.68 | Mn2+ | 86% activity compared to Mg2+ | Haloferax volcanii | |
| 3.1.1.68 | additional information | the enzyme requires divalent cations for activity | Haloferax volcanii | |
| 3.1.1.68 | Ni2+ | 21% activity compared to Mg2+ | Haloferax volcanii | |
| 3.1.1.68 | Zn2+ | 14% activity compared to Mg2+ | Haloferax volcanii | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.68 | 28000 | - |
recombinant His-tagged enzyme, gel filtration | Haloferax volcanii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.4.11 | Francisella tularensis subsp. holarctica | A0A0B6CP33 | - |
- |
| 1.8.4.12 | Francisella tularensis subsp. holarctica | A0A0B3VNT0 | - |
- |
| 3.1.1.68 | Haloferax volcanii | D4GP31 | - |
- |
| 3.1.1.68 | Haloferax volcanii ATCC 29605 | D4GP31 | - |
- |
| 3.1.1.68 | Haloferax volcanii DS2 | D4GP31 | - |
- |
| 3.1.1.68 | Haloferax volcanii DSM 3757 | D4GP31 | - |
- |
| 3.1.1.68 | Haloferax volcanii JCM 8879 | D4GP31 | - |
- |
| 3.1.1.68 | Haloferax volcanii NBRC 14742 | D4GP31 | - |
- |
| 3.1.1.68 | Haloferax volcanii NCIMB 2012 | D4GP31 | - |
- |
| 3.1.1.68 | Haloferax volcanii VKM B-1768 | D4GP31 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.68 | recombinant His-tagged enzyme from Haloferax volcanii strain H1209 by nickel affinity chromatography and gel filtration to homogeneity | Haloferax volcanii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii | D-xylonate | - |
? | |
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii NCIMB 2012 | D-xylonate | - |
? | |
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii JCM 8879 | D-xylonate | - |
? | |
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii DS2 | D-xylonate | - |
? | |
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii DSM 3757 | D-xylonate | - |
? | |
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii ATCC 29605 | D-xylonate | - |
? | |
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii NBRC 14742 | D-xylonate | - |
? | |
| 3.1.1.68 | D-xylono-1,4-lactone + H2O | preferred substrate | Haloferax volcanii VKM B-1768 | D-xylonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii | L-arabinonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii NCIMB 2012 | L-arabinonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii JCM 8879 | L-arabinonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii DS2 | L-arabinonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii DSM 3757 | L-arabinonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii ATCC 29605 | L-arabinonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii NBRC 14742 | L-arabinonate | - |
? | |
| 3.1.1.68 | L-arabinono-1,4-lactone + H2O | about 50% activity compared to D-xylono-1,4-lactone | Haloferax volcanii VKM B-1768 | L-arabinonate | - |
? | |
| 3.1.1.68 | 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 | ? | - |
? | |
| 3.1.1.68 | 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 | ? | - |
? | |
| 3.1.1.68 | 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 | ? | - |
? | |
| 3.1.1.68 | 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 | ? | - |
? | |
| 3.1.1.68 | 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 | ? | - |
? | |
| 3.1.1.68 | 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 | ? | - |
? | |
| 3.1.1.68 | 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 | ? | - |
? | |
| 3.1.1.68 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.1.68 | monomer | 1 * 31400, about, sequence calculation, 1 * 35000, recombinant His-tagged enzyme, SDS-PAGE | Haloferax volcanii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.68 | D-xylonolactonase | - |
Haloferax volcanii |
| 3.1.1.68 | HVO_B0030 | - |
Haloferax volcanii |
| 3.1.1.68 | lactonase | - |
Haloferax volcanii |
| 3.1.1.68 | More | cf. EC 3.1.1.15 | Haloferax volcanii |
| 3.1.1.68 | pentonolactonase | - |
Haloferax volcanii |
| 3.1.1.68 | XacC | - |
Haloferax volcanii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.68 | 42 | - |
assay at | Haloferax volcanii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.68 | 7.5 | - |
assay at | Haloferax volcanii |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 3.1.1.68 | Haloferax volcanii | gene xacC is transcriptionally induced by both L-arabinose and D-xylose, and the regulator XacR | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.8.4.11 | physiological function | an msrA mutant displays little difference with wild-type strain. A double mutant lacking both MsrB, EC 1.8.1.12, and MsrA exhibits the same characteristics as the MsrB mutant. The bacterial count of the MsrA mutant is lower than that of the wild-type strain in the liver, but not in the spleen, of mice | Francisella tularensis subsp. holarctica |
| 1.8.4.12 | physiological function | an mMrB mutant exhibits decreased in vitro growth, exogenous oxidative stress resistance and intracellular growth in macrophages. A double mutant lacking both MsrA, EC 1.8.1.11, and MsrB exhibits the same characteristics as the MsrB mutant. The bacterial count of the MsrB mutant is significantly lower than that of the wild-type strain in the liver and spleen of mice | Francisella tularensis subsp. holarctica |
| 3.1.1.68 | 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 |
| 3.1.1.68 | 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]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.68 | 10.74 | - |
L-arabinono-1,4-lactone | pH 7.5, 42°C, recombinant enzyme | Haloferax volcanii | |
| 3.1.1.68 | 20.96 | - |
D-xylono-1,4-lactone | pH 7.5, 42°C, recombinant enzyme | Haloferax volcanii | |
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