EzCatDB: D00060

DB codeD00060
CATH domainDomain 11.10.520.10Catalytic domain
Domain 21.10.420.10Catalytic domain
E.C.1.11.1.11
CSA1apx

CATH domainRelated DB codes (homologues)
1.10.420.10D00061,D00062
1.10.520.10D00061,D00062

Enzyme Name
Swiss-protKEGG

P48534Q43758
Protein nameL-ascorbate peroxidase, cytosolic
L-ascorbate peroxidase
L-ascorbic acid peroxidase
L-ascorbic acid-specific peroxidase
ascorbate peroxidase
ascorbic acid peroxidase
SynonymsAP
EC 1.11.1.11
PsAPx01
Ascorbate peroxidase
EC 1.11.1.11
Cytosolic ascorbate peroxidase 1
EC 1.11.1.11

KEGG pathways
MAP codePathways
MAP00053Ascorbate and aldarate metabolism
MAP00480Glutathione metabolism

Swiss-prot:Accession NumberP48534Q43758
Entry nameAPX1_PEAQ43758_SOYBN
ActivityL-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O.
Subunit

Subcellular locationCytoplasm.
CofactorBinds 1 heme B (iron-protoporphyrin IX) group per subunit.,Binds 1 potassium or calcium ion per subunit.


CofactorsSubstratesProducts
KEGG-idC00032C00076C00238C00072C00027C05422C00001
CompoundHemeCalciumPotassiumL-AscorbateH2O2DehydroascorbateH2O
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metaldivalent metal (Ca2+, Mg2+)univalent metal (Na+, K+)carbohydrate,aromatic ring (with hetero atoms other than nitrogen atoms)otherscarbohydrateH2O
1apxA01UnboundUnboundUnboundUnboundUnboundUnbound
1apxB01UnboundUnboundUnboundUnboundUnboundUnbound
1apxC01UnboundUnboundUnboundUnboundUnboundUnbound
1apxD01UnboundUnboundUnboundUnboundUnboundUnbound
1oafA01UnboundUnboundUnboundBound:ASCUnboundUnbound
1oagA01UnboundUnboundUnboundUnboundUnboundUnbound
1v0hX01UnboundUnboundUnboundAnalogue:SHAUnboundUnbound
1apxA02Bound:HEMUnboundBound:__KUnboundUnboundUnbound
1apxB02Bound:HEMUnboundBound:__KUnboundUnboundUnbound
1apxC02Bound:HEMUnboundBound:__KUnboundUnboundUnbound
1apxD02Bound:HEMUnboundBound:__KUnboundUnboundUnbound
1oafA02Bound:HEMUnboundAnalogue:_NAUnboundUnboundUnbound
1oagA02Bound:HEMUnboundUnboundUnboundUnboundUnbound
1v0hX02Bound:HEMUnboundAnalogue:_NAUnboundUnboundUnbound

Active-site residues
resource
PDB;1apx & Swiss-prot;P48534 & literature [26], [27], [29], [33]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
1apxA01CYS 32;ARG 38;HIS 42

TRP 41
1apxB01CYS 32;ARG 38;HIS 42

TRP 41
1apxC01CYS 32;ARG 38;HIS 42

TRP 41
1apxD01CYS 32;ARG 38;HIS 42

TRP 41
1oafA01CYS 32;ARG 38;HIS 42

TRP 41
1oagA01CYS 32;ARG 38;HIS 42

TRP 41
1v0hX01CYS 32;ARG 38;HIS 42

TRP 41
1apxA02ARG 172;ASP 208
HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding)
TRP 179
1apxB02ARG 172;ASP 208
HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding)
TRP 179
1apxC02ARG 172;ASP 208
HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding)
TRP 179
1apxD02ARG 172;ASP 208
HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding)
TRP 179
1oafA02ARG 172;ASP 208
HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding)
TRP 179
1oagA02ARG 172;ASP 208
HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding)
TRP 179
1v0hX02ARG 172;ASP 208
HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding)
TRP 179

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[13]

[19]

[21]p.329-339
[26]

[27]

[29]Scheme 1
[31]Fig.10, p.371-376
[32]p.304-306
[33]Scheme 1, p.32-35
[34]p.8649-8650

references
[1]
PubMed ID1915856
JournalFEBS Lett
Year1991
Volume289
Pages257-9
AuthorsMittler R, Zilinskas BA
TitleMolecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase.
[2]
PubMed ID1400489
JournalJ Biol Chem
Year1992
Volume267
Pages21802-7
AuthorsMittler R, Zilinskas BA
TitleMolecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase.
[3]
PubMed ID8422923
JournalFEBS Lett
Year1993
Volume315
Pages313-7
AuthorsKubo A, Saji H, Tanaka K, Kondo N
TitleGenomic DNA structure of a gene encoding cytosolic ascorbate peroxidase from Arabidopsis thaliana.
[4]
PubMed ID8006006
JournalJ Biol Chem
Year1994
Volume269
Pages17020-4
AuthorsPatterson WR, Poulos TL
TitleCharacterization and crystallization of recombinant pea cytosolic ascorbate peroxidase.
[5]
PubMed ID7672248
JournalBiochem Soc Trans
Year1995
Volume23
Pages228-32
AuthorsPoulos TL, Patterson WR, Sundaramoorthy M
TitleThe crystal structure of ascorbate and manganese peroxidases: the role of non-haem metal in the catalytic mechanism.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID95217899
PubMed ID7703247
JournalBiochemistry
Year1995
Volume34
Pages4331-41
AuthorsPatterson WR, Poulos TL
TitleCrystal structure of recombinant pea cytosolic ascorbate peroxidase.
Related PDB1apx
Related Swiss-protP48534
[7]
PubMed ID8638916
JournalArch Biochem Biophys
Year1996
Volume328
Pages1-8
AuthorsDalton DA, Diaz del Castillo L, Kahn ML, Joyner SL, Chatfield JM
TitleHeterologous expression and characterization of soybean cytosolic ascorbate peroxidase.
[8]
PubMed ID8766820
JournalFEBS Lett
Year1996
Volume389
Pages153-6
AuthorsMarquez LA, Quitoriano M, Zilinskas BA, Dunford HB
TitleKinetic and spectral properties of pea cytosolic ascorbate peroxidase.
[9]
PubMed ID9291097
JournalBiochem J
Year1997
Volume326
Pages305-10
AuthorsJespersen HM, Kjaersgard IV, Ostergaard L, Welinder KG
TitleFrom sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase.
[10]
PubMed ID9346287
JournalEur J Biochem
Year1997
Volume248
Pages347-54
AuthorsHill AP, Modi S, Sutcliffe MJ, Turner DD, Gilfoyle DJ, Smith AT, Tam BM, Lloyd E
TitleChemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase.
[11]
PubMed ID9144965
JournalPlant Cell
Year1997
Volume9
Pages627-40
AuthorsKarpinski S, Escobar C, Karpinska B, Creissen G, Mullineaux PM
TitlePhotosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress.
[12]
PubMed ID9578600
JournalArch Biochem Biophys
Year1998
Volume353
Pages55-63
AuthorsYoshimura K, Ishikawa T, Nakamura Y, Tamoi M, Takeda T, Tada T, Nishimura K, Shigeoka S
TitleComparative study on recombinant chloroplastic and cytosolic ascorbate peroxidase isozymes of spinach.
[13]
PubMed ID9860877
JournalBiochemistry
Year1998
Volume37
Pages17610-7
AuthorsMandelman D, Jamal J, Poulos TL
TitleIdentification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography.
[14]
PubMed ID9609702
JournalBiochemistry
Year1998
Volume37
Pages8080-7
AuthorsNissum M, Neri F, Mandelman D, Poulos TL, Smulevich G
TitleSpectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: similarities and differences with cytochrome c peroxidase.
[15]
PubMed ID9443387
JournalPlanta
Year1998
Volume204
Pages120-6
AuthorsCaldwell CR, Turano FJ, McMahon MB
TitleIdentification of two cytosolic ascorbate peroxidase cDNAs from soybean leaves and characterization of their products by functional expression in E. coli.
[16]
PubMed ID9792095
JournalProtein Sci
Year1998
Volume7
Pages2089-98
AuthorsMandelman D, Schwarz FP, Li H, Poulos TL
TitleThe role of quaternary interactions on the stability and activity of ascorbate peroxidase.
[17]
PubMed ID10217180
JournalElectrophoresis
Year1999
Volume20
Pages630-6
AuthorsKomatsu S, Muhammad A, Rakwal R
TitleSeparation and characterization of proteins from green and etiolated shoots of rice (Oryza sativa L.): towards a rice proteome.
[18]
PubMed ID10729193
JournalArch Biochem Biophys
Year2000
Volume376
Pages82-90
AuthorsTakeda T, Yoshimura K, Yoshii M, Kanahoshi H, Miyasaka H, Shigeoka S
TitleMolecular characterization and physiological role of ascorbate peroxidase from halotolerant Chlamydomonas sp. W80 strain.
[19]
PubMed ID10858284
JournalBiochemistry
Year2000
Volume39
Pages7374-9
AuthorsBursey EH, Poulos TL
TitleTwo substrate binding sites in ascorbate peroxidase: the role of arginine 172.
[20]
PubMed ID11128006
JournalPhilos Trans R Soc Lond B Biol Sci
Year2000
Volume355
Pages1531-40
AuthorsMullineaux P, Ball L, Escobar C, Karpinska B, Creissen G, Karpinski S
TitleAre diverse signalling pathways integrated in the regulation of arabidopsis antioxidant defence gene expression in response to excess excitation energy?
[21]
PubMed ID11192727
JournalSubcell Biochem
Year2000
Volume35
Pages317-49
AuthorsRaven EL
TitlePeroxidase-catalyzed oxidation of ascorbate. Structural, spectroscopic and mechanistic correlations in ascorbate peroxidase.
[22]
PubMed ID11361125
JournalArch Biochem Biophys
Year2001
Volume388
Pages100-12
AuthorsBattistuzzi G, D'Onofrio M, Loschi L, Sola M
TitleIsolation and characterization of two peroxidases from Cucumis sativus.
[23]
PubMed ID11356136
JournalBiochem Soc Trans
Year2001
Volume29
Pages105-11
AuthorsLloyd Raven E, Celik A, Cullis PM, Sangar R, Sutcliffe MJ
TitleEngineering the active site of ascorbate peroxidase.
[24]
PubMed ID11696974
JournalDNA Seq
Year2001
Volume11
Pages475-84
AuthorsKim IJ, Lee BH, Jo J, Chung WI
TitleSequence variability of nine cytosolic ascorbate peroxidases in polyploid strawberry.
[25]
PubMed ID11121105
JournalEur J Biochem
Year2001
Volume268
Pages78-85
AuthorsCelik A, Cullis PM, Sutcliffe MJ, Sangar R, Raven EL
TitleEngineering the active site of ascorbate peroxidase.
[26]
PubMed ID11358529
JournalEur J Biochem
Year2001
Volume268
Pages3091-8
AuthorsHiner AN, Martinez JI, Arnao MB, Acosta M, Turner DD, Lloyd Raven E, Rodriguez-Lopez JN
TitleDetection of a tryptophan radical in the reaction of ascorbate peroxidase with hydrogen peroxide.
[27]
PubMed ID12427040
JournalBiochemistry
Year2002
Volume41
Pages13774-81
AuthorsLad L, Mewies M, Raven EL
TitleSubstrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites.
[28]
PubMed ID12506974
JournalBiosci Biotechnol Biochem
Year2002
Volume66
Pages2367-75
AuthorsKitajima S, Ueda M, Sano S, Miyake C, Kohchi T, Tomizawa K, Shigeoka S, Yokota A
TitleStable form of ascorbate peroxidase from the red alga Galdieria partita similar to both chloroplastic and cytosolic isoforms of higher plants.
[29]
PubMed ID12084058
JournalEur J Biochem
Year2002
Volume269
Pages3182-92
AuthorsLad L, Mewies M, Basran J, Scrutton NS, Raven EL
TitleRole of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants.
[30]
PubMed ID12966073
JournalJ Biochem (Tokyo)
Year2003
Volume134
Pages239-44
AuthorsWada K, Tada T, Nakamura Y, Ishikawa T, Yabuta Y, Yoshimura K, Shigeoka S, Nishimura K
TitleCrystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability.
[31]
PubMed ID12964833
JournalNat Prod Rep
Year2003
Volume20
Pages367-81
AuthorsRaven EL
TitleUnderstanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?
[32]
PubMed ID12640445
JournalNat Struct Biol
Year2003
Volume10
Pages303-7
AuthorsSharp KH, Mewies M, Moody PC, Raven EL
TitleCrystal structure of the ascorbate peroxidase-ascorbate complex.
Related PDB1oaf,1oag
[33]
PubMed ID15777010
JournalBiochem Soc Symp
Year2004
Volume(71)
Pages27-38
AuthorsRaven EL, Lad L, Sharp KH, Mewies M, Moody PC
TitleDefining substrate specificity and catalytic mechanism in ascorbate peroxidase.
[34]
PubMed ID15236572
JournalBiochemistry
Year2004
Volume43
Pages8644-51
AuthorsSharp KH, Moody PC, Brown KA, Raven EL
TitleCrystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex.
Related PDB1v0h

comments
According to the literature, this enzyme catalyzes three successive reactions:
(A) Enzyme + H2O2 => Enzyme Intermediate I + H2O
(B) Enzyme Intermediate I + AH => Enzyme Intermediate II + A*
(C) Enzyme Intermediate II + AH => Enzyme + A* + H2O
Here, AH is substrate, ascorbate, whereas A* is a radical form of ascorbate. Enzyme Intermediate I contains oxyferryl [Fe(IV)=O].

createdupdated
2004-05-112009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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