Information on EC 3.1.1.27 - 4-pyridoxolactonase

for references in articles please use BRENDA:EC3.1.1.27
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.27
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RECOMMENDED NAME
GeneOntology No.
4-pyridoxolactonase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-pyridoxolactone + H2O = 4-pyridoxate
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vitamin B6 degradation
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Vitamin B6 metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
4-pyridoxolactone lactonohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37278-41-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MA-1
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-pyridoxate
4-pyridoxolactone + H2O
show the reaction diagram
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-
-
-
r
4-pyridoxolactone + H2O
4-pyridoxate
show the reaction diagram
4-Pyridoxolactone + H2O
?
show the reaction diagram
-
vitamin B6 degradation
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-
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N-hexanoyl-D,L-homoserine lactone + H2O
N-hexanoyl-D,L-homoserine
show the reaction diagram
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41% of the activity with 4-pyridoxolactone
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-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-pyridoxolactone + H2O
4-pyridoxate
show the reaction diagram
Q988B9
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-
-
?
4-Pyridoxolactone + H2O
?
show the reaction diagram
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vitamin B6 degradation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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1,7-phenanthroline
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4-Pyridoxolactone
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substrate inhibition above 0. 02 mM
5-Pyridoxolactone
Hg2+
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0.1 mM, complete inhibition
p-chloromercuribenzoate
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p-phenanthroline
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.319
4-pyridoxate
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pH 7.5
0.0031 - 0.008
4-Pyridoxolactone
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
4-pyridoxate
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pH 7.5
12.2
4-Pyridoxolactone
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pH 7.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
5-Pyridoxolactone
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pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
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5
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36% of maximum activity
5.9 - 8.7
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50% of maximal activity at pH 5.9 and pH 8.7
9.5
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10% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
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2 * 28000, SDS-PAGE
29855
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2 * 31000, SDS-PAGE, 2 * 29855, calculated
54000
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gel filtration
59000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
additional information
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N-terminal amino acid sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the sitting-drop vapour-diffusion method, at 4°C. Free enzyme to 2.0 A resolution, belongs to the monoclinic space group C2, with unit-cell parameters a = 77.93, b = 38.88, c = 81.60 A, beta = 117.33. The 5-pyridoxolactone-bound enzyme to 1.9 A resolution, belongs to the monoclinic space group C2, with unit-cell parameters a = 86.24, b = 39.35, c = 82.68 A, beta = 118.02
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native and SeMet-labelled protein in complex with 5-pyridoxolactone, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 50 mM ammonium citrate, pH 5.1
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
10 min, stable
55
-
10 min, 64% residual activity
60
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10 min, 14% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme shows very low activity in Tris-HCl bufffers
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography, hydroxyapatite column chromatography, and Shodex protein KW-803 gel filtration
recombinant enzyme purified sequentially by gel filtration and ammonium sulfate precipitation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834 (DE3) cells
overexpressed in Escherichia coli BL21 (DE3) cells harbouring plasmid pET21a6805
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