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1.11.1.11: L-ascorbate peroxidase

This is an abbreviated version!
For detailed information about L-ascorbate peroxidase, go to the full flat file.

Word Map on EC 1.11.1.11

Reaction

2 L-ascorbate +

H2O2
+ 2 H+ = 2 monodehydroascorbate + 2 H2O

Synonyms

Am-pAPX1, APEX2, APOX, APX, APX 1, APX 2, APX1, APX2, APX3, APX4, APX5, APX6, APX7, APx8, APXS, APXT, ascorbate peroxidase, ascorbate peroxidase 1, ascorbate peroxidase 2, ascorbate peroxidase 3, ascorbate peroxidase 4, ascorbate peroxidase 5, ascorbate peroxidase 6, ascorbate peroxidase 7, ascorbate peroxidase 8, ascorbate peroxidase6, ascorbic acid peroxidase, At1g07890, AT1G77490, AT3G09640, AT4G08390, AT4G32320, AT4G35000, AT4G35970, AtAPx08, AtAPX1, AtAPX2, AtAPX3, AtAPX5, AtAPX6, AtSAPX, AtstAPX, AtTAPX, cAPX, cAPX 2, CmstAPX, CrAPX4, CreAPX1, CreAPX2, CreAPX4, CreAPXheme, CsAPX1, cytoplasmic ascorbate peroxidase 1, cytosolic ascorbate peroxidase, GhAPX1, glyoxysomal APX, HvAPX1, L-ascorbate peroxidase, L-ascorbate peroxidase 3, L-ascorbate peroxidase 5, L-ascorbate peroxidase 6, L-ascorbate peroxidase, heme-containing, L-ascorbic acid peroxidase, L-ascorbic acid-specific peroxidase, LmAPX, MaAPX1, OsAPx1, OsAPx2, OsAPx3, OsAPx4, OsAPx5, OsAPx6, OsAPx7, OsAPx8, OsAPXa, OsAPXb, pAPX, Pavirv00022559m, peroxidase, ascorbate, peroxisomal ascorbate peroxidase, PgAPX1, PHYPA_001206, PHYPA_001884, PHYPA_021776, PHYPA_024580, PHYPA_024582, Potri.002G081900, Potri.004G174500, Potri.005G112200, Potri.005G161900, Potri.005G179200, Potri.006G089000, Potri.006G132200, Potri.006G254500, Potri.009G015400, Potri.009G134100, Potri.016G084800, PpAPX, PpAPX-S, PpAPX2, PpAPX2.1, PpAPX2.2, PpAPX3, PpAPX6-related, PtAPX-S.1, PtAPX-S.2, PtAPX-TL29, PtAPX.3, PtAPX1.1, PtAPX1.2, PtAPX2, PtAPX3, PtAPX5, PtAPX5-like, PtAPX6 related, PtotAPX, RcAPX, sAPX, stromal APX, stromal ascorbate peroxidase, stromal ascorbate peroxidases, TaAPX, tAPX, thylakoid ascorbate peroxidase, thylakoid membrane-bound ascorbate peroxidases, thylakoid-bound ascorbate peroxidase

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.11 L-ascorbate peroxidase

Specific Activity

Specific Activity on EC 1.11.1.11 - L-ascorbate peroxidase

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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000264
-
the specific activity of the purified native enzyme is very low, pH 7.0, 25°C
0.039 - 0.055
-
different samples grown at different temperatures from 14-34°C, assay at pH 7.2, 25°C
0.048 - 0.06
-
different samples grown at different temperatures from 14-34°C, assay at pH 7.2, 25°C
0.092
-
crude extract of root nodules
0.096
-
crude extract of root nodules, cv Alaska
0.1
-
purified enzyme
0.11
-
crude extract of root nodules
0.161
-
crude extract of root nodules, cv Austrian winter
0.206
-
pH 7.2, 25°C
0.213
-
crude extract of root nodules
0.241
-
crude extract of root nodules
0.258
-
crude extract of root nodules
0.26
-
effect of abscisic acid and EGTA on APX activity, 1 day following chilling stress
0.27
-
effect of abscisic acid and EGTA on APX activity, 7 days, under normal temperature
0.284
-
crude extract of root nodules
0.35
-
in water, 4 days, under normal temperature
0.366
-
crude extract of root nodules
0.37
-
effect of LaCl3 on APX activity, 4 days, under normal temperature
0.4
-
effect of abscisic acid on APX activity, 1 day following chilling stress
0.45
-
effect of abscisic acid on APX activity, 4 days, under normal temperature
0.625
light-grown culture, pH 7.2, 25°C. No activity in the dark-grown culture
0.7684
-
crude extract
1.3
Chlamydomonas sp.
recombinant enzyme, soluble fraction, addition of 3% NaCl
1.6
-
crude extract, in 50 mM potassium phosphate (pH 7.0), at 22°C
100
-
cytosolic enzyme, in the presence and absence of salicylic acid
117
-
purified recombinant enzyme
1307
-
purified enzyme
132.2
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: cumene hydroperoxide
142.1
-
purified enzyme, electron donor: D-araboascorbic acid, electron acceptor: H2O2
1500
-
chloroplastic enzyme, in the presence and absence of salicylic acid
172.8
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: tert-butyl hydroperoxide
185.5
-
purified enzyme, electron donor: pyrogallol, electron acceptor: H2O2
19.2
-
substrate: tert-butyl hydroperoxide
2.8
-
purified enzyme, electron donor: glutathione, electron acceptor: H2O2
20.3
-
purified enzyme, electron donor: guaiacol, electron acceptor: H2O2
20.9
-
substrate: H2O2
254
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: H2O2
3 - 4
-
affinity purified preparation
3.3
-
cell extract
31.7
-
purified recombinant enzyme
32
-
recombinant enzyme
34
-
wild-type enzyme
34.2
-
purified enzyme
36
-
purified enzyme
37
-
stress factor drought
378
-
pH 7.5, 25°C
4.32
-
crude extract of root nodules, activity is only detected when soluble polyvinylpolypyrrolidone is included in the buffer and O2 is excluded by through degassing of buffers and performing all extraction steps under a vigorous stream of N2 gas
456
-
after 285fold purification, in 50 mM potassium phosphate (pH 7.0), at 22°C
46.7
-
partially purified enzyme
5.8
-
purified enzyme, electron donor: iodide, electron acceptor: H2O2
53
-
stress factors drought and heat
56
-
purified enzyme
561.1
-
purified enzyme
580
Chlamydomonas sp.
purified recombinant enzyme
63.6
-
recombinant enzyme 2, after chromatofocusing
636
Chlamydomonas sp.
purified native enzyme
7.1
-
substrate: cumene hydroperoxide
9.4
-
recombinant enzyme 1, after DEAE-column chromatography
additional information