DB code: D00060

CATH domain 1.10.520.10 : Peroxidase; domain 1 Catalytic domain
1.10.420.10 : Peroxidase; domain 2 Catalytic domain
E.C. 1.11.1.11
CSA 1apx
M-CSA 1apx
MACiE

CATH domain Related DB codes (homologues)
1.10.520.10 : Peroxidase; domain 1 D00061 D00062
1.10.420.10 : Peroxidase; domain 2 D00061 D00062

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
P48534 L-ascorbate peroxidase, cytosolic
AP
EC 1.11.1.11
PsAPx01
PF00141 (peroxidase)
[Graphical View]
Q43758
Ascorbate peroxidase
EC 1.11.1.11
Cytosolic ascorbate peroxidase 1
EC 1.11.1.11
Uncharacterized protein
PF00141 (peroxidase)
[Graphical View]
NP_001237785.1 (Protein)
NM_001250856.1 (DNA/RNA sequence)

KEGG enzyme name
L-ascorbate peroxidase
L-ascorbic acid peroxidase
L-ascorbic acid-specific peroxidase
ascorbate peroxidase
ascorbic acid peroxidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q43758 Q43758_SOYBN
P48534 APX1_PEA L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O. Cytoplasm. Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Binds 1 potassium or calcium ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00480 Glutathione metabolism
MAP00053 Ascorbate and aldarate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00032 C00076 C00238 C00072 C00027 C05422 C00001
E.C.
Compound Heme Calcium Potassium L-Ascorbate H2O2 Dehydroascorbate H2O
Type aromatic ring (with nitrogen atoms),carboxyl group,heavy metal divalent metal (Ca2+, Mg2+) univalent metal (Na+, K+) carbohydrate,aromatic ring (with hetero atoms other than nitrogen atoms) others carbohydrate H2O
ChEBI 17627
26355
29108
29103
29073
16240
27956
15377
PubChem 271
813
54670067
22326046
784
440667
22247451
962
1apxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1apxB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1apxC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1apxD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1oafA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:ASC Unbound Unbound
1oagA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1v0hX01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:SHA Unbound Unbound
1apxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Bound:__K Unbound Unbound Unbound
1apxB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Bound:__K Unbound Unbound Unbound
1apxC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Bound:__K Unbound Unbound Unbound
1apxD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Bound:__K Unbound Unbound Unbound
1oafA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Analogue:_NA Unbound Unbound Unbound
1oagA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound
1v0hX02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Analogue:_NA Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1apx & Swiss-prot;P48534 & literature [26], [27], [29], [33]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1apxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 32;ARG 38;HIS 42 TRP 41
1apxB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 32;ARG 38;HIS 42 TRP 41
1apxC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 32;ARG 38;HIS 42 TRP 41
1apxD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 32;ARG 38;HIS 42 TRP 41
1oafA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 32;ARG 38;HIS 42 TRP 41
1oagA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 32;ARG 38;HIS 42 TRP 41
1v0hX01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 32;ARG 38;HIS 42 TRP 41
1apxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 172;ASP 208 HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding) TRP 179
1apxB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 172;ASP 208 HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding) TRP 179
1apxC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 172;ASP 208 HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding) TRP 179
1apxD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 172;ASP 208 HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding) TRP 179
1oafA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 172;ASP 208 HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding) TRP 179
1oagA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 172;ASP 208 HIS 163(Heme binding);THR 164;THR 180;ASN 182;ILE 185;ASP 187(Potassium or Calcium binding) TRP 179
1v0hX02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 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
References Sections No. 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]
Resource
Comments
Medline ID
PubMed ID 1915856
Journal FEBS Lett
Year 1991
Volume 289
Pages 257-9
Authors Mittler R, Zilinskas BA
Title Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1400489
Journal J Biol Chem
Year 1992
Volume 267
Pages 21802-7
Authors Mittler R, Zilinskas BA
Title Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8422923
Journal FEBS Lett
Year 1993
Volume 315
Pages 313-7
Authors Kubo A, Saji H, Tanaka K, Kondo N
Title Genomic DNA structure of a gene encoding cytosolic ascorbate peroxidase from Arabidopsis thaliana.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8006006
Journal J Biol Chem
Year 1994
Volume 269
Pages 17020-4
Authors Patterson WR, Poulos TL
Title Characterization and crystallization of recombinant pea cytosolic ascorbate peroxidase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7672248
Journal Biochem Soc Trans
Year 1995
Volume 23
Pages 228-32
Authors Poulos TL, Patterson WR, Sundaramoorthy M
Title The crystal structure of ascorbate and manganese peroxidases: the role of non-haem metal in the catalytic mechanism.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 95217899
PubMed ID 7703247
Journal Biochemistry
Year 1995
Volume 34
Pages 4331-41
Authors Patterson WR, Poulos TL
Title Crystal structure of recombinant pea cytosolic ascorbate peroxidase.
Related PDB 1apx
Related UniProtKB P48534
[7]
Resource
Comments
Medline ID
PubMed ID 8638916
Journal Arch Biochem Biophys
Year 1996
Volume 328
Pages 1-8
Authors Dalton DA, Diaz del Castillo L, Kahn ML, Joyner SL, Chatfield JM
Title Heterologous expression and characterization of soybean cytosolic ascorbate peroxidase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8766820
Journal FEBS Lett
Year 1996
Volume 389
Pages 153-6
Authors Marquez LA, Quitoriano M, Zilinskas BA, Dunford HB
Title Kinetic and spectral properties of pea cytosolic ascorbate peroxidase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9291097
Journal Biochem J
Year 1997
Volume 326
Pages 305-10
Authors Jespersen HM, Kjaersgard IV, Ostergaard L, Welinder KG
Title From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9346287
Journal Eur J Biochem
Year 1997
Volume 248
Pages 347-54
Authors Hill AP, Modi S, Sutcliffe MJ, Turner DD, Gilfoyle DJ, Smith AT, Tam BM, Lloyd E
Title Chemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9144965
Journal Plant Cell
Year 1997
Volume 9
Pages 627-40
Authors Karpinski S, Escobar C, Karpinska B, Creissen G, Mullineaux PM
Title Photosynthetic electron transport regulates the expression of cytosolic ascorbate peroxidase genes in Arabidopsis during excess light stress.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 9578600
Journal Arch Biochem Biophys
Year 1998
Volume 353
Pages 55-63
Authors Yoshimura K, Ishikawa T, Nakamura Y, Tamoi M, Takeda T, Tada T, Nishimura K, Shigeoka S
Title Comparative study on recombinant chloroplastic and cytosolic ascorbate peroxidase isozymes of spinach.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9860877
Journal Biochemistry
Year 1998
Volume 37
Pages 17610-7
Authors Mandelman D, Jamal J, Poulos TL
Title Identification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9609702
Journal Biochemistry
Year 1998
Volume 37
Pages 8080-7
Authors Nissum M, Neri F, Mandelman D, Poulos TL, Smulevich G
Title Spectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: similarities and differences with cytochrome c peroxidase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9443387
Journal Planta
Year 1998
Volume 204
Pages 120-6
Authors Caldwell CR, Turano FJ, McMahon MB
Title Identification of two cytosolic ascorbate peroxidase cDNAs from soybean leaves and characterization of their products by functional expression in E. coli.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9792095
Journal Protein Sci
Year 1998
Volume 7
Pages 2089-98
Authors Mandelman D, Schwarz FP, Li H, Poulos TL
Title The role of quaternary interactions on the stability and activity of ascorbate peroxidase.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 10217180
Journal Electrophoresis
Year 1999
Volume 20
Pages 630-6
Authors Komatsu S, Muhammad A, Rakwal R
Title Separation and characterization of proteins from green and etiolated shoots of rice (Oryza sativa L.): towards a rice proteome.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 10729193
Journal Arch Biochem Biophys
Year 2000
Volume 376
Pages 82-90
Authors Takeda T, Yoshimura K, Yoshii M, Kanahoshi H, Miyasaka H, Shigeoka S
Title Molecular characterization and physiological role of ascorbate peroxidase from halotolerant Chlamydomonas sp. W80 strain.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 10858284
Journal Biochemistry
Year 2000
Volume 39
Pages 7374-9
Authors Bursey EH, Poulos TL
Title Two substrate binding sites in ascorbate peroxidase: the role of arginine 172.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 11128006
Journal Philos Trans R Soc Lond B Biol Sci
Year 2000
Volume 355
Pages 1531-40
Authors Mullineaux P, Ball L, Escobar C, Karpinska B, Creissen G, Karpinski S
Title Are diverse signalling pathways integrated in the regulation of arabidopsis antioxidant defence gene expression in response to excess excitation energy?
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 11192727
Journal Subcell Biochem
Year 2000
Volume 35
Pages 317-49
Authors Raven EL
Title Peroxidase-catalyzed oxidation of ascorbate. Structural, spectroscopic and mechanistic correlations in ascorbate peroxidase.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 11361125
Journal Arch Biochem Biophys
Year 2001
Volume 388
Pages 100-12
Authors Battistuzzi G, D'Onofrio M, Loschi L, Sola M
Title Isolation and characterization of two peroxidases from Cucumis sativus.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 11356136
Journal Biochem Soc Trans
Year 2001
Volume 29
Pages 105-11
Authors Lloyd Raven E, Celik A, Cullis PM, Sangar R, Sutcliffe MJ
Title Engineering the active site of ascorbate peroxidase.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 11696974
Journal DNA Seq
Year 2001
Volume 11
Pages 475-84
Authors Kim IJ, Lee BH, Jo J, Chung WI
Title Sequence variability of nine cytosolic ascorbate peroxidases in polyploid strawberry.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 11121105
Journal Eur J Biochem
Year 2001
Volume 268
Pages 78-85
Authors Celik A, Cullis PM, Sutcliffe MJ, Sangar R, Raven EL
Title Engineering the active site of ascorbate peroxidase.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 11358529
Journal Eur J Biochem
Year 2001
Volume 268
Pages 3091-8
Authors Hiner AN, Martinez JI, Arnao MB, Acosta M, Turner DD, Lloyd Raven E, Rodriguez-Lopez JN
Title Detection of a tryptophan radical in the reaction of ascorbate peroxidase with hydrogen peroxide.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 12427040
Journal Biochemistry
Year 2002
Volume 41
Pages 13774-81
Authors Lad L, Mewies M, Raven EL
Title Substrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 12506974
Journal Biosci Biotechnol Biochem
Year 2002
Volume 66
Pages 2367-75
Authors Kitajima S, Ueda M, Sano S, Miyake C, Kohchi T, Tomizawa K, Shigeoka S, Yokota A
Title Stable form of ascorbate peroxidase from the red alga Galdieria partita similar to both chloroplastic and cytosolic isoforms of higher plants.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 12084058
Journal Eur J Biochem
Year 2002
Volume 269
Pages 3182-92
Authors Lad L, Mewies M, Basran J, Scrutton NS, Raven EL
Title Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 12966073
Journal J Biochem (Tokyo)
Year 2003
Volume 134
Pages 239-44
Authors Wada K, Tada T, Nakamura Y, Ishikawa T, Yabuta Y, Yoshimura K, Shigeoka S, Nishimura K
Title Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 12964833
Journal Nat Prod Rep
Year 2003
Volume 20
Pages 367-81
Authors Raven EL
Title Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 12640445
Journal Nat Struct Biol
Year 2003
Volume 10
Pages 303-7
Authors Sharp KH, Mewies M, Moody PC, Raven EL
Title Crystal structure of the ascorbate peroxidase-ascorbate complex.
Related PDB 1oaf 1oag
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 15777010
Journal Biochem Soc Symp
Year 2004
Volume (71)
Pages 27-38
Authors Raven EL, Lad L, Sharp KH, Mewies M, Moody PC
Title Defining substrate specificity and catalytic mechanism in ascorbate peroxidase.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 15236572
Journal Biochemistry
Year 2004
Volume 43
Pages 8644-51
Authors Sharp KH, Moody PC, Brown KA, Raven EL
Title Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex.
Related PDB 1v0h
Related UniProtKB

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].

Created Updated
2004-05-11 2009-02-26