Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase and Organism(s) Mycobacterium tuberculosis and UniProt Accession O06553

for references in articles please use BRENDA:EC1.4.3.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A flavoprotein (FMN). In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). N4'-Substituted pyridoxamine derivatives are also oxidized in reaction (1) to form pyridoxal 5-phosphate and the corresponding primary amine.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: O06553
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyridoxine 5'-phosphate oxidase, pnpox, pyridoxine phosphate oxidase, pyridox(am)ine 5'-phosphate oxidase, pnp oxidase, pyridoxine-5'-phosphate oxidase, pyridoxamine 5'-phosphate oxidase, pyridoxamine phosphate oxidase, pyridoxine (pyridoxamine) phosphate oxidase, pyridoxine (pyridoxamine) 5'-phosphate oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyridoxine 5'-phosphate oxidase
-
FprA protein
-
-
-
-
oxidase, pyridoxamine phosphate
-
-
-
-
PMP oxidase
-
-
-
-
PNP/PMP oxidase
-
-
-
-
PNPOx
pyridoxamine 5'-phosphate oxidase
-
-
-
-
pyridoxamine phosphate oxidase
-
-
-
-
pyridoxamine-phosphate oxidase
-
-
-
-
pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating)
-
-
-
-
pyridoxine (pyridoxamine) 5'-phosphate oxidase
-
-
-
-
pyridoxine (pyridoxamine) phosphate oxidase
-
-
-
-
pyridoxine 5'-phosphate oxidase
-
-
pyridoxine/pyridoxamine 5'-phosphate oxidase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pyridoxamine-5'-phosphate:oxygen oxidoreductase (deaminating)
A flavoprotein (FMN). In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). N4'-Substituted pyridoxamine derivatives are also oxidized in reaction (1) to form pyridoxal 5-phosphate and the corresponding primary amine.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-21-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme does not recognize pyridoxamine 5'-phosphate as substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme does not recognize pyridoxamine 5'-phosphate as substrate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
-
contains one FMN molecule per dimer
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36
pyridoxine 5'-phosphate
-
in 25 mM potassium phosphate, pH 7.8 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
pyridoxine 5'-phosphate
-
in 25 mM potassium phosphate, pH 7.8 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028
pyridoxine 5'-phosphate
-
in 25 mM potassium phosphate, pH 7.8 and 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
-
x * 15000, recombinant detagged enzyme, SDS-PAGE
27000
-
2 * 27000, SDS-PAGE
54000
-
gel filtration
55380
-
nano-ESI mass spectroscopy
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 15000, recombinant detagged enzyme, SDS-PAGE
homodimer
-
2 * 27000, SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme from strain Rv1155, sitting drop vapour diffusion method, 9 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 25-50 mM KF, and 10 mM glutathione, mixed with an equal volume of precipitation solution containing 0.1 M HEPES, pH 7.5, 8% ethylene glycol, and 10% PEG 8000, macroseeding with hanging drops containing equal volumes of protein and precipitation solutions overnight prior to seeding, 1-2 weeks, cryoprotection by 30% ethylene glycol, X-ray diffraction structure determination and analysis at 1.7-2.2 A, modeling
purified recombinant enzyme from strain Rv2074, sitting drop vapour diffusion method in microtiter plates at room temperature, 12 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 5 mM DTT, and glutathione, mixed with an equal volume of precipitation solution containing 0.2 M sodium citrate, pH 5.0, 30% glycerol, and 20% PEG 4000, hanging drop vapour diffusion with 0.5 ml protein and 1 ml precipitation solutions mixed, 1-2 weeks, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.0 A, modeling
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, removal of the GST-tag by rTEV protease, followed by dialysis and ultrafiltration
HisTrap nickel-affinity column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography
-
recombinant GST-tagged wild-type and of GST-tagged selenomethionine-labeled enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, removal of the GST-tags by rTEV protease, followed by dialysis and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the GST-tagged enzyme from strain Rv1155 in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
-
expression of GST-tagged wild-type and of GST-tagged selenomethionine-labeled enzymes from strain Rv2074 in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Biswal, B.K.; Cherney, M.M.; Wang, M.; Garen, C.; James, M.N.
Structures of Mycobacterium tuberculosis pyridoxine 5'-phosphate oxidase and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate
Acta Crystallogr. Sect. D
61
1492-1499
2005
Mycobacterium tuberculosis (O06553), Mycobacterium tuberculosis
Manually annotated by BRENDA team
Biswal, B.K.; Au, K.; Cherney, M.M.; Garen, C.; James, M.N.
The molecular structure of Rv2074, a probable pyridoxine 5'-phosphate oxidase from Mycobacterium tuberculosis, at 1.6 angstroms resolution
Acta Crystallogr. Sect. F
62
735-742
2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis Rv2074
Manually annotated by BRENDA team
Mashalidis, E.H.; Mukherjee, T.; Sled?, P.; Matak-Vinkovi?, D.; Boshoff, H.; Abell, C.; Barry, C.E.
Rv2607 from Mycobacterium tuberculosis is a pyridoxine 5-phosphate oxidase with unusual substrate specificity
PLoS ONE
6
e27643
2011
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Sathish Kumar, M.; Jaleel, U.
Molecular docking studies of PA-824 with pyridoxine 5'-phosphate oxidase
Biol. Med. (Aligarh)
8
274
2016
Mycobacterium tuberculosis (O06553)
-
Manually annotated by BRENDA team
Ankisettypalli, K.; Cheng, J.J.; Baker, E.N.; Bashiri, G.
PdxH proteins of Mycobacteria are typical members of the classical pyridoxine/pyridoxamine 5-phosphate oxidase family
FEBS Lett.
590
453-460
2016
Mycobacterium marinum (B2HF83), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis (A0R420), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0R420)
Manually annotated by BRENDA team