1.4.3.5: pyridoxal 5'-phosphate synthase
This is an abbreviated version!
For detailed information about pyridoxal 5'-phosphate synthase, go to the full flat file.
Word Map on EC 1.4.3.5
Reaction
Synonyms
ePNPOx, FprA protein, oxidase, pyridoxamine phosphate, Pdx1, PDX3, PdxH, PMP oxidase, PNP oxidase, PNP/PMP oxidase, PNPO, PNPOx, PPOX, pyridox(am)ine 5'-phosphate oxidase, pyridoxal 5'-phosphate synthase, pyridoxal 5'-phosphate synthetic enzyme, pyridoxamine (pyridoxine) 5'-phosphate oxidase, pyridoxamine (pyridoxine) 5’-phosphate:O2 oxidoreductase (deaminating), pyridoxamine 5'-phosphate oxidase, pyridoxamine phosphate oxidase, pyridoxamine-5-phosphate oxidase, pyridoxamine-phosphate oxidase, pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating), pyridoxinamine 5'-phosphate oxidase, pyridoxine (pyridoxamine) 5 '-phosphate oxidase, pyridoxine (pyridoxamine) 5'-phosphate oxidase, pyridoxine (pyridoxamine) phosphate oxidase, pyridoxine 5'-phosphate oxidase, pyridoxine 5'-phosphate oxidase`, pyridoxine 5-phosphate oxidase, pyridoxine phosphate oxidase, pyridoxine-5'-phosphate oxidase, pyridoxine/pyridoxamine 5'-phosphate oxidase, pyridoxine/pyridoxamine phosphate oxidase, sgll, Sgll/PNPO, Ylr456w, Ypr172w
ECTree
1.4.3.5 pyridoxal 5'-phosphate synthaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-(propan-2-yl)-6-[2-[4-(propan-2-yl)phenoxy]ethoxy]-1,3-dihydro-2H-benzimidazol-2-one
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1-ethyl-6-[2-(3-fluorophenoxy)ethoxy]-1,3-dihydro-2H-benzimidazol-2-one
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1-ethyl-6-[2-[4-(propan-2-yl)phenoxy]ethoxy]-1,3-dihydro-2H-benzimidazol-2-one
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1-ethyl-6-[[4-(trifluoromethyl)phenyl]methoxy]-1,3-dihydro-2H-benzimidazol-2-one
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1-methyl-6-(3-phenylpropoxy)-1,3-dihydro-2H-benzimidazol-2-one
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2,3-Butanedione
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10 mM, complete inhibition after 50 min in borate buffer, inhibition is fully reversible upon removal of borate
5-[(3,4-dichlorophenyl)methoxy]-1,3-dihydro-2H-indol-2-one
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5-[(3,4-dichlorophenyl)methoxy]-3,3-dimethyl-1,3-dihydro-2H-indol-2-one
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5-[(3-chlorophenyl)methoxy]-3,3-dimethyl-1,3-dihydro-2H-indol-2-one
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5-[(3-fluorophenyl)methoxy]-3-(propan-2-yl)-1,3-dihydro-2H-indol-2-one
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6-[(3,4-dichlorophenyl)methoxy]-1-methyl-1,3-dihydro-2H-benzimidazol-2-one
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6-[(3-chlorophenyl)methoxy]-1-methyl-1,3-dihydro-2H-benzimidazol-2-one
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6-[(4-chlorophenyl)methoxy]-1-methyl-1,3-dihydro-2H-benzimidazol-2-one
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ammonium sulfate
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1.9 M, E II: activation at short incubation time, E I: complete inactivation after 10 h incubation; inactivation of isozyme E-I after 10 h
diethyldicarbonate
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1.2 mM, complete inactivation after 10 min, activity decrease of 60% can be restored by a 20 min incubation with 900 mM hydroxylamine, pyridoxal 5'-phosphate oxime protects from inactivation, inactivation is due to modification of histidine residues
Fe2+
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2.85 mM, 44% inhibition of pyridoxamine 5'-phosphate oxidation, 81% inhibition of pyridoxine oxidation
Fe3+
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2.85 mM, 26% inhibition of pyridoxamine 5'-phosphate oxidation, 50% inhibition of pyridoxine oxidation
Urea
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both activates and denatures the enzyme, reversible inactivation above 2.5 M, half-time of inactivation is 46 min at 2 M and 37°C
Cd2+
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2.85 mM, 82% inhibition of pyridoxamine 5'-phosphate oxidation, 27% inhibition of pyridoxine oxidation
Cd2+
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0.5 mM, isozyme E I: insensitive, isozyme E II: 44% inhibition; 44% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Cu2+
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2.85 mM, 38% inhibition of pyridoxamine 5'-phosphate oxidation, 23% inhibition of pyridoxine oxidation
Hg2+
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2.85 mM, 30% inhibition of pyridoxamine 5'-phosphate oxidation, 2% inhibition of pyridoxine oxidation
Hg2+
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0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
pyridoxal 5'-phosphate
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product inhibition is of a mixed-type nature and results from binding of this vitamer at an allosteric site
pyridoxal 5'-phosphate
the enzyme undergoes an allosteric feedback inhibition by pyridoxal 5'-phosphate (PLP) caused by a strong allosteric coupling between PLP binding at the allosteric site and substrate binding at the active site. One PLP molecule is bound at the allosteric site of one monomer
pyridoxal 5'-phosphate
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competitive inhibition; competitive product inhibition, overview
Zn2+
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2.85 mM, 92% inhibition of pyridoxamine 5'-phosphate oxidation, 60% inhibition of pyridoxine oxidation
Zn2+
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0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
additional information
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pyridoxamine 5'-phosphate shows no substrate inhibition
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additional information
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no substrate inhibition with pyridoxamine 5'-phosphate
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