KEGG   ENZYME: 1.11.1.11Help
Entry
EC 1.11.1.11                Enzyme                                 

Name
L-ascorbate peroxidase;
L-ascorbic acid peroxidase;
L-ascorbic acid-specific peroxidase;
ascorbate peroxidase;
ascorbic acid peroxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
BRITE hierarchy
Sysname
L-ascorbate:hydrogen-peroxide oxidoreductase
Reaction(IUBMB)
2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O (overall reaction) [RN:R00644];
(1a) 2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O [RN:R09540];
(1b) 2 monodehydroascorbate = L-ascorbate + L-dehydroascorbate (spontaneous) [RN:R03186]
Reaction(KEGG)
Substrate
L-ascorbate [CPD:C00072];
H2O2 [CPD:C00027];
H+ [CPD:C00080];
monodehydroascorbate [CPD:C01041]
Product
L-ascorbate [CPD:C00072];
L-dehydroascorbate [CPD:C05422];
H2O [CPD:C00001];
monodehydroascorbate [CPD:C01041]
Comment
A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymic disproportionation to ascorbate and dehydroascorbate.
History
EC 1.11.1.11 created 1983, modified 2010, modified 2011
Pathway
ec00053  Ascorbate and aldarate metabolism
ec00480  Glutathione metabolism
Orthology
K00434  L-ascorbate peroxidase
Genes
RSS: 109441715 109442257 109442717
ATH: AT1G07890(APX1) AT1G77490(TAPX) AT3G09640(APX2) AT4G08390(SAPX) AT4G09010(TL29) AT4G32320(APX6) AT4G35000(APX3) AT4G35970(APX5)
ALY: ARALYDRAFT_470824 ARALYDRAFT_476914 ARALYDRAFT_478284 ARALYDRAFT_489709 ARALYDRAFT_489749 ARALYDRAFT_491040 ARALYDRAFT_491157 ARALYDRAFT_898677 ARALYDRAFT_899988 ARALYDRAFT_899989 ARALYDRAFT_901951 ARALYDRAFT_913218
CRB: 17878438 17879152 17880619 17884052 17884559 17890815 17893627 17893747 17896270 17899405
CSAT: 104702532 104707160 104707215 104713416 104716524 104716637 104716949 104719794 104720283 104721287 104727620 104729589 104729717 104730042 104736879 104736925 104739373 104745137 104747469 104747470 104751645 104754395 104754965 104764660 104765991 104766972 104766975 104792024 104792033
EUS: EUTSA_v10008402mg EUTSA_v10018581mg EUTSA_v10021381mg EUTSA_v10022797mg EUTSA_v10023023mg EUTSA_v10025686mg EUTSA_v10025911mg EUTSA_v10025942mg EUTSA_v10028739mg EUTSA_v10028759mg
BRP: 103832195(tapx) 103836413 103838791(sapx) 103843426(apx2) 103848043 103858501 103860476 103862119 103862385 103871533(APX) 103871729
BNA: 106346376 106346377 106347996 106354606 106362267 106386647 106389449 106401842 106407140 106415142 106419633 106420215 106422138 106423276 106427935 106428784 106433208 106435662 106435671 106435674 106438471 106439834 106446154 106446926 111199406 111207743
BOE: 106294764 106300129 106303893 106306187 106307224 106308404 106312994 106324757 106324893 106328411 106328985
THJ: 104800618 104803658 104804273 104804329 104813110 104813151 104813669 104815756 104816316 104826354
LJA: Lj1g3v0250130.2(Lj1g3v0250130.2) Lj1g3v0839140.1(Lj1g3v0839140.1) Lj1g3v0839140.2(Lj1g3v0839140.2) Lj1g3v1901620.1(Lj1g3v1901620.1) Lj3g3v3465510.1(Lj3g3v3465510.1)
DOSA: Os02t0553200-01(Os02g0553200) Os03t0285700-01(Os03g0285700) Os04t0223300-00(Os04g0223300) Os04t0434800-01(Os04g0434800) Os04t0602100-01(Os04g0602100) Os07t0694700-01(Os07g0694700) Os08t0522400-01(Os08g0522400) Os08t0549100-01(Os08g0549100) Os12t0178100-01(Os12g0178100) Os12t0178200-01(Os12g0178200)
ATS: 109739529(LOC109739529) 109747802(LOC109747802) 109748346(LOC109748346) 109749043(LOC109749043) 109749624(LOC109749624) 109757934(LOC109757934) 109771362(LOC109771362) 109785628(LOC109785628) 109786189(LOC109786189)
SMIN: v1.2.015684.t1(symbB.v1.2.015684.t1) v1.2.018236.t1(symbB.v1.2.018236.t1) v1.2.018679.t1(symbB.v1.2.018679.t1) v1.2.024207.t2(symbB.v1.2.024207.t2) v1.2.024207.t3(symbB.v1.2.024207.t3) v1.2.028328.t1(symbB.v1.2.028328.t1) v1.2.032093.t1(symbB.v1.2.032093.t1)
FCY: FRACYDRAFT_173923(APX1)
LMA: LMJF_34_0070(APX)
LIF: LINJ_34_0070(APX)
LBZ: LBRM_20_0150(APX)
 » show all
Taxonomy
Reference
1  [PMID:6772104]
  Authors
Shigeoka S, Nakano Y, Kitaoka S.
  Title
Purification and some properties of L-ascorbic-acid-specific peroxidase in Euglena gracilis Z.
  Journal
Arch Biochem Biophys 201:121-7 (1980)
DOI:10.1016/0003-9861(80)90495-6
Reference
2  [PMID:6768357]
  Authors
Shigeoka S, Nakano Y, Kitaoka S.
  Title
Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase.
  Journal
Biochem J 186:377-80 (1980)
Reference
3
  Authors
Nakano, Y and Asada, K.
  Title
Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical.
  Journal
Plant Cell Physiol 28:131-140 (1987)
Reference
4  [PMID:7703247]
  Authors
Patterson WR, Poulos TL
  Title
Crystal structure of recombinant pea cytosolic ascorbate peroxidase.
  Journal
Biochemistry 34:4331-41 (1995)
Reference
5  [PMID:15236572]
  Authors
Sharp KH, Moody PC, Brown KA, Raven EL
  Title
Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex.
  Journal
Biochemistry 43:8644-51 (2004)
DOI:10.1021/bi049343q
  Sequence
[gmx:553156]
Reference
6  [PMID:16784232]
  Authors
Macdonald IK, Badyal SK, Ghamsari L, Moody PC, Raven EL
  Title
Interaction of ascorbate peroxidase with substrates: a mechanistic and structural analysis.
  Journal
Biochemistry 45:7808-17 (2006)
DOI:10.1021/bi0606849
  Sequence
[gmx:553156]
Other DBs
ExplorEnz - The Enzyme Database: 1.11.1.11
IUBMB Enzyme Nomenclature: 1.11.1.11
ExPASy - ENZYME nomenclature database: 1.11.1.11
BRENDA, the Enzyme Database: 1.11.1.11
CAS: 72906-87-7

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