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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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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
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vitamin B6 degradation
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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
ORGANISM
UNIPROT
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
Rhizobium loti (strain MAFF303099)
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
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10 min, stable
55
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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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