DB code: D00870

RLCP classification	3.676.249900.37 : Transfer
CATH domain	3.40.30.10 : Glutaredoxin	Catalytic domain
CATH domain	3.30.1020.10 : Antioxidant, Horf6; Chain A, domain 2
E.C.	1.11.1.15
CSA
M-CSA
MACiE

CATH domain	Related DB codes (homologues)
3.40.30.10 : Glutaredoxin	S00916 S00279 M00184 D00866 D00869 D00278

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	Pfam
Q86SB3		1-Cys peroxiredoxin	PF10417 (1-cysPrx_C) PF00578 (AhpC-TSA) [Graphical View]

KEGG enzyme name
Peroxiredoxin Thioredoxin peroxidase Tryparedoxin peroxidase Alkyl hydroperoxide reductase C22 AhpC TrxPx TXNPx Prx PRDX

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
Q86SB3	Q86SB3_9APIC

KEGG Pathways
Map code	Pathways	E.C.

Compound table
	Substrates		Products			Intermediates
KEGG-id	C16736	C15498	C15496	C00001	C01335	I00142	I00143
E.C.
Compound	R'-SH	ROOH	R-S-S-R	H2O	ROH	Peptidyl-Cys-sulfenic acid	Transient disulfide bond between peptidyl-Cys
Type	sulfhydryl group	others	disulfide bond	H2O	carbohydrate
ChEBI				15377 15377
PubChem				22247451 962 22247451 962

1xccA01	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
1xccB01	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
1xccC01	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
1xccD01	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
3tb2A01	Unbound	Unbound	Unbound		Unbound	Intermediate-analogue:CSD	Unbound
3tb2B01	Unbound	Unbound	Unbound		Unbound	Intermediate-analogue:CSD	Unbound
3tb2C01	Unbound	Unbound	Unbound		Unbound	Intermediate-analogue:CSD	Unbound
3tb2D01	Unbound	Unbound	Unbound		Unbound	Intermediate-analogue:CSD	Unbound
1xccA02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
1xccB02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
1xccC02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
1xccD02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
3tb2A02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
3tb2B02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
3tb2C02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
3tb2D02	Unbound	Unbound	Unbound		Unbound	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
Literature [1], [2], [4], [5], [6]

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1xccA01	THR 44;CYS 47;ARG 129			ASN 41;VAL 46;CYS 47
1xccB01	THR 44;CYS 47;ARG 129			ASN 41;VAL 46;CYS 47
1xccC01	THR 44;CYS 47;ARG 129			ASN 41;VAL 46;CYS 47
1xccD01	THR 44;CYS 47;ARG 129			ASN 41;VAL 46;CYS 47
3tb2A01	THR 44; ;ARG 129		CSD 47(3-Sulfinoalanine)	ASN 41;VAL 46;CYS 47
3tb2B01	THR 44; ;ARG 129		CSD 47(3-Sulfinoalanine)	ASN 41;VAL 46;CYS 47
3tb2C01	THR 44; ;ARG 129		CSD 47(3-Sulfinoalanine)	ASN 41;VAL 46;CYS 47
3tb2D01	THR 44; ;ARG 129		CSD 47(3-Sulfinoalanine)	ASN 41;VAL 46;CYS 47
1xccA02
1xccB02
1xccC02
1xccD02
3tb2A02
3tb2B02
3tb2C02
3tb2D02

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[1]	Fig. 4
[2]	Fig. 1

References
[1]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID
PubMed ID	9587003
Journal	Nat Struct Biol
Year	1998
Volume	5
Pages	400-6
Authors	Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE
Title	Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Related PDB	1prx
Related UniProtKB	P30041
[2]
Resource
Comments
Medline ID
PubMed ID	12517450
Journal	Trends Biochem Sci
Year	2003
Volume	28
Pages	32-40
Authors	Wood ZA, Schroder E, Robin Harris J, Poole LB
Title	Structure, mechanism and regulation of peroxiredoxins.
Related PDB
Related UniProtKB
[3]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SULFINATION AT CYS-47.
Medline ID
PubMed ID	17125854
Journal	Mol Biochem Parasitol
Year	2007
Volume	151
Pages	100-10
Authors	Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R
Title	Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Related PDB	1xcc 3tb2
Related UniProtKB	Q86SB3
[4]
Resource
Comments
Medline ID
PubMed ID	18084889
Journal	Subcell Biochem
Year	2007
Volume	44
Pages	41-60
Authors	Karplus PA, Hall A
Title	Structural survey of the peroxiredoxins.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID	20969484
Journal	Antioxid Redox Signal
Year	2011
Volume	15
Pages	795-815
Authors	Hall A, Nelson K, Poole LB, Karplus PA
Title	Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID	22429898
Journal	BMC Struct Biol
Year	2012
Volume	12
Pages	2
Authors	Qiu W, Dong A, Pizarro JC, Botchkarsev A, Min J, Wernimont AK, Hills T, Hui R, Artz JD
Title	Crystal structures from the Plasmodium peroxiredoxins: new insights into oligomerization and product binding.
Related PDB
Related UniProtKB

Comments
Peroxiredoxins (Prxs) can be classified into three categories (see [2]): (1) typical 2-Cys Prxs; conservation of two redox-active cysteines; homodimers having two identical active sites. (2) atypical 2-Cys Prxs; conservation of two redox-active cysteines; functionally monomeric. (3) 1-Cys Prxs; only one cysteine. This enzyme belongs to the category of 1-Cys Prxs. The redox-active cysteine is referred to as the peroxidatic cysteine, in contrast to the second cysteine, the resolving cysteine, in the 2-Cys Prxs. Since this enzyme is homologous to 1-Cys Prxs (D00869, S00916 in EzCatDB) with a similar active site, it must have a similar catalytic mechanism as the homologue. Thus, this enzyme catalyzes the following reactions (see [2]): (A) Transfer of peroxide oxygen from another peroxide oxygen to the perdoxidatic Cys, forming Cys-sulfenic acid: (B) Transfer of sulfur atom of the peroxidatic Cys from the hydroxyl group to thiol (or sulfhydryl) group of the second substrat (C) Electron transfer from thiol of the third substrate (or another R'-SH) to the disulfide bond (thiol-disulfide exchange): Although this enzyme can be over-oxidized to form sulfinic acid (-SO2H) and further oxidized sulfonic acid (-SO3H), over-oxidization mechanism is not described in this entry. Incidentally, 3tb2 (of PDB) gives structures of sulfinic acid form.

Comments

Peroxiredoxins (Prxs) can be classified into three categories (see [2]):
(1) typical 2-Cys Prxs; conservation of two redox-active cysteines; homodimers having two identical active sites.
(2) atypical 2-Cys Prxs; conservation of two redox-active cysteines; functionally monomeric.
(3) 1-Cys Prxs; only one cysteine.
This enzyme belongs to the category of 1-Cys Prxs.
The redox-active cysteine is referred to as the peroxidatic cysteine, in contrast to the second cysteine, the resolving cysteine, in the 2-Cys Prxs.
Since this enzyme is homologous to 1-Cys Prxs (D00869, S00916 in EzCatDB) with a similar active site, it must have a similar catalytic mechanism as the homologue.
Thus, this enzyme catalyzes the following reactions (see [2]):
(A) Transfer of peroxide oxygen from another peroxide oxygen to the perdoxidatic Cys, forming Cys-sulfenic acid:
(B) Transfer of sulfur atom of the peroxidatic Cys from the hydroxyl group to thiol (or sulfhydryl) group of the second substrat
(C) Electron transfer from thiol of the third substrate (or another R'-SH) to the disulfide bond (thiol-disulfide exchange):
Although this enzyme can be over-oxidized to form sulfinic acid (-SO2H) and further oxidized sulfonic acid (-SO3H), over-oxidization mechanism is not described in this entry. Incidentally, 3tb2 (of PDB) gives structures of sulfinic acid form.

Created	Updated
2012-07-12	2012-09-13