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Literature summary for 1.4.3.5 extracted from

  • Tsuge, H.; Kuroda, Y.; Iwamoto, A.; Ohashi, K.
    Partial purification and property of pyridoxine (pyridoxamine)-5-phosphate oxidase isozymes from wheat seedlings (1982), Arch. Biochem. Biophys., 217, 479-484.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ammonium sulfate short incubation activates isozyme E-II, not E-I Triticum aestivum

Inhibitors

Inhibitors Comment Organism Structure
ammonium sulfate 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 Triticum aestivum
Cd2+ 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 Triticum aestivum
citrate-phosphate buffer
-
Triticum aestivum
Hg2+ 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 Triticum aestivum
Zn2+ 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 Triticum aestivum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0067
-
pyridoxamine 5'-phosphate isozyme E-II, pH 8.0, 37°C Triticum aestivum
0.008
-
pyridoxine 5'-phosphate isozyme E-II, pH 8.0, 37°C Triticum aestivum
0.02
-
pyridoxine 5'-phosphate isozyme E-I, pH 8.0, 37°C Triticum aestivum

Organism

Organism UniProt Comment Textmining
Triticum aestivum
-
isozymes: E1 and E2
-
Triticum aestivum
-
two isozymes E-I and E-II
-

Purification (Commentary)

Purification (Comment) Organism
two isozymes from seedlings, partially by anion exchange and adsorption chromatography Triticum aestivum

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
Triticum aestivum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00188
-
isozyme EII Triticum aestivum
0.00367
-
isozyme EI Triticum aestivum
0.113
-
purified isozyme E-II, substrate pyridoxine 5'-phosphate Triticum aestivum
0.45
-
purified isozyme E-I, substrate pyridoxine 5'-phosphate Triticum aestivum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+ 1.6fold preferred substrate of isozyme E-II Triticum aestivum pyridoxal 5'-phosphate + FMNH2 + NH3
-
?
pyridoxamine 5'-phosphate + H2O + O2 E II uses pyridoxine 5'-phosphate and pyridoxamine 5'-phosphate Triticum aestivum pyridoxal 5'-phosphate + NH3 + H2O2
-
?
pyridoxamine 5'-phosphate + H2O + O2 isozymes E I uses only pyridoxine 5'-phosphate as substrate Triticum aestivum pyridoxal 5'-phosphate + NH3 + H2O2
-
?
pyridoxine 5'-phosphate + FMN 9fold preferred substrate of isozyme E-I Triticum aestivum pyridoxal 5'-phosphate + FMNH2
-
?

Synonyms

Synonyms Comment Organism
pyridoxamine (pyridoxine) 5'-phosphate oxidase
-
Triticum aestivum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Triticum aestivum
40
-
isozymes EI and EII, rapid decrease above Triticum aestivum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
rapid decrease in activity above 40°C, both isozymes Triticum aestivum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
-
Triticum aestivum
9.5
-
both isozymes Triticum aestivum

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.1
-
37°C, 30 min, isozyme E I: 85% loss of activity, isozyme E II: 50% loss of activity Triticum aestivum

Cofactor

Cofactor Comment Organism Structure
FMN
-
Triticum aestivum

pI Value

Organism Comment pI Value Maximum pI Value
Triticum aestivum the pI values of the isozymes differ from each other
-
additional information