EzCatDB: T00021

DB codeT00021
CATH domainDomain 12.40.180.10Catalytic domain
Domain 21.10.422.10
Domain 33.40.50.880
E.C.1.11.1.6
CSA1iph

CATH domainRelated DB codes (homologues)
3.40.50.880D00526,M00215,T00114

Enzyme Name
Swiss-protKEGG

P21179
Protein nameCatalase HPIIcatalase
equilase
caperase
optidase
catalase-peroxidase
CAT
SynonymsEC 1.11.1.6
Hydroxyperoxidase II

KEGG pathways
MAP codePathways
MAP00380Tryptophan metabolism
MAP00680Methane metabolism

Swiss-prot:Accession NumberP21179
Entry nameCATE_ECOLI
Activity2 H(2)O(2) = O(2) + 2 H(2)O.
SubunitHomotetramer.
Subcellular locationCytoplasm (Probable).
CofactorHeme group.


CofactorsSubstratesProductsintermediates
KEGG-idC00032C00027C00007C00001


CompoundHemeH2O2O2H2OCompound I Covalent-bonded Tyr415-His392Heme hydroxychlorin spirolactone + covalent-bonded Tyr415-His392
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metalothersothersH2O


1cf9A01Bound:HEMUnboundUnbound

UnboundUnbound
1cf9B01Bound:HEMUnboundUnbound

UnboundUnbound
1cf9C01Bound:HEMUnboundUnbound

UnboundUnbound
1cf9D01Bound:HEMUnboundUnbound

UnboundUnbound
1gg9A01Bound:HEMUnboundUnbound

UnboundUnbound
1gg9B01Bound:HEMUnboundUnbound

UnboundUnbound
1gg9C01Bound:HEMUnboundUnbound

UnboundUnbound
1gg9D01Bound:HEMUnboundUnbound

UnboundUnbound
1ggeA01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggeB01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggeC01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggeD01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggfA01Bound:HEMBound:2xPEOUnbound

UnboundUnbound
1ggfB01Bound:HEMBound:2xPEOUnbound

UnboundUnbound
1ggfC01Bound:HEMBound:2xPEOUnbound

UnboundUnbound
1ggfD01Bound:HEMBound:2xPEOUnbound

UnboundUnbound
1gghA01Bound:HEMUnboundUnbound

UnboundUnbound
1gghB01Bound:HEMUnboundUnbound

UnboundUnbound
1gghC01Bound:HEMUnboundUnbound

UnboundUnbound
1gghD01Bound:HEMUnboundUnbound

UnboundUnbound
1ggjA01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggjB01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggjC01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggjD01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1ggkA01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1ggkB01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1ggkC01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1ggkD01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1iphA01Bound:HEMUnboundUnbound

UnboundUnbound
1iphB01Bound:HEMUnboundUnbound

UnboundUnbound
1iphC01Bound:HEMUnboundUnbound

UnboundUnbound
1iphD01Bound:HEMUnboundUnbound

UnboundUnbound
1p7yA01Bound:HEMUnboundUnbound

UnboundUnbound
1p7yB01Bound:HEMUnboundUnbound

UnboundUnbound
1p7yC01Bound:HEMUnboundUnbound

UnboundUnbound
1p7yD01Bound:HEMUnboundUnbound

UnboundUnbound
1p7zA01Bound:HEMUnboundUnbound

UnboundUnbound
1p7zB01Bound:HEMUnboundUnbound

UnboundUnbound
1p7zC01Bound:HEMUnboundUnbound

UnboundUnbound
1p7zD01Bound:HEMUnboundUnbound

UnboundUnbound
1p80A01Bound:HEMUnboundUnbound

UnboundUnbound
1p80B01Bound:HEMUnboundUnbound

UnboundUnbound
1p80C01Bound:HEMUnboundUnbound

UnboundUnbound
1p80D01Bound:HEMUnboundUnbound

UnboundUnbound
1p81A01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1p81B01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1p81C01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1p81D01Analogue:HDDUnboundUnbound

UnboundIntermediate-bound:HDD-TYR 415-HIS 392
1qf7A01Bound:HEMUnboundUnbound

UnboundUnbound
1qf7B01Bound:HEMUnboundUnbound

UnboundUnbound
1qf7C01Bound:HEMUnboundUnbound

UnboundUnbound
1qf7D01Bound:HEMUnboundUnbound

UnboundUnbound
1qwsA01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1qwsB01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1qwsC01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1qwsD01Bound:HEMUnboundUnbound

Intermediate-bound:TYR 415-HIS 392Unbound
1cf9A02UnboundUnboundUnbound

UnboundUnbound
1cf9B02UnboundUnboundUnbound

UnboundUnbound
1cf9C02UnboundUnboundUnbound

UnboundUnbound
1cf9D02UnboundUnboundUnbound

UnboundUnbound
1gg9A02UnboundUnboundUnbound

UnboundUnbound
1gg9B02UnboundUnboundUnbound

UnboundUnbound
1gg9C02UnboundUnboundUnbound

UnboundUnbound
1gg9D02UnboundUnboundUnbound

UnboundUnbound
1ggeA02UnboundUnboundUnbound

UnboundUnbound
1ggeB02UnboundUnboundUnbound

UnboundUnbound
1ggeC02UnboundUnboundUnbound

UnboundUnbound
1ggeD02UnboundUnboundUnbound

UnboundUnbound
1ggfA02UnboundBound:PEOUnbound

UnboundUnbound
1ggfB02UnboundBound:PEOUnbound

UnboundUnbound
1ggfC02UnboundBound:PEOUnbound

UnboundUnbound
1ggfD02UnboundBound:PEOUnbound

UnboundUnbound
1gghA02UnboundUnboundUnbound

UnboundUnbound
1gghB02UnboundUnboundUnbound

UnboundUnbound
1gghC02UnboundUnboundUnbound

UnboundUnbound
1gghD02UnboundUnboundUnbound

UnboundUnbound
1ggjA02UnboundUnboundUnbound

UnboundUnbound
1ggjB02UnboundUnboundUnbound

UnboundUnbound
1ggjC02UnboundUnboundUnbound

UnboundUnbound
1ggjD02UnboundUnboundUnbound

UnboundUnbound
1ggkA02UnboundUnboundUnbound

UnboundUnbound
1ggkB02UnboundUnboundUnbound

UnboundUnbound
1ggkC02UnboundUnboundUnbound

UnboundUnbound
1ggkD02UnboundUnboundUnbound

UnboundUnbound
1iphA02UnboundUnboundUnbound

UnboundUnbound
1iphB02UnboundUnboundUnbound

UnboundUnbound
1iphC02UnboundUnboundUnbound

UnboundUnbound
1iphD02UnboundUnboundUnbound

UnboundUnbound
1p7yA02UnboundUnboundUnbound

UnboundUnbound
1p7yB02UnboundUnboundUnbound

UnboundUnbound
1p7yC02UnboundUnboundUnbound

UnboundUnbound
1p7yD02UnboundUnboundUnbound

UnboundUnbound
1p7zA02UnboundUnboundUnbound

UnboundUnbound
1p7zB02UnboundUnboundUnbound

UnboundUnbound
1p7zC02UnboundUnboundUnbound

UnboundUnbound
1p7zD02UnboundUnboundUnbound

UnboundUnbound
1p80A02UnboundUnboundUnbound

UnboundUnbound
1p80B02UnboundUnboundUnbound

UnboundUnbound
1p80C02UnboundUnboundUnbound

UnboundUnbound
1p80D02UnboundUnboundUnbound

UnboundUnbound
1p81A02UnboundUnboundUnbound

UnboundUnbound
1p81B02UnboundUnboundUnbound

UnboundUnbound
1p81C02UnboundUnboundUnbound

UnboundUnbound
1p81D02UnboundUnboundUnbound

UnboundUnbound
1qf7A02UnboundUnboundUnbound

UnboundUnbound
1qf7B02UnboundUnboundUnbound

UnboundUnbound
1qf7C02UnboundUnboundUnbound

UnboundUnbound
1qf7D02UnboundUnboundUnbound

UnboundUnbound
1qwsA02UnboundUnboundUnbound

UnboundUnbound
1qwsB02UnboundUnboundUnbound

UnboundUnbound
1qwsC02UnboundUnboundUnbound

UnboundUnbound
1qwsD02UnboundUnboundUnbound

UnboundUnbound
1cf9A03UnboundUnboundUnbound

UnboundUnbound
1cf9B03UnboundUnboundUnbound

UnboundUnbound
1cf9C03UnboundUnboundUnbound

UnboundUnbound
1cf9D03UnboundUnboundUnbound

UnboundUnbound
1gg9A03UnboundUnboundUnbound

UnboundUnbound
1gg9B03UnboundUnboundUnbound

UnboundUnbound
1gg9C03UnboundUnboundUnbound

UnboundUnbound
1gg9D03UnboundUnboundUnbound

UnboundUnbound
1ggeA03UnboundUnboundUnbound

UnboundUnbound
1ggeB03UnboundUnboundUnbound

UnboundUnbound
1ggeC03UnboundUnboundUnbound

UnboundUnbound
1ggeD03UnboundUnboundUnbound

UnboundUnbound
1ggfA03UnboundUnboundUnbound

UnboundUnbound
1ggfB03UnboundUnboundUnbound

UnboundUnbound
1ggfC03UnboundUnboundUnbound

UnboundUnbound
1ggfD03UnboundUnboundUnbound

UnboundUnbound
1gghA03UnboundUnboundUnbound

UnboundUnbound
1gghB03UnboundUnboundUnbound

UnboundUnbound
1gghC03UnboundUnboundUnbound

UnboundUnbound
1gghD03UnboundUnboundUnbound

UnboundUnbound
1ggjA03UnboundUnboundUnbound

UnboundUnbound
1ggjB03UnboundUnboundUnbound

UnboundUnbound
1ggjC03UnboundUnboundUnbound

UnboundUnbound
1ggjD03UnboundUnboundUnbound

UnboundUnbound
1ggkA03UnboundUnboundUnbound

UnboundUnbound
1ggkB03UnboundUnboundUnbound

UnboundUnbound
1ggkC03UnboundUnboundUnbound

UnboundUnbound
1ggkD03UnboundUnboundUnbound

UnboundUnbound
1iphA03UnboundUnboundUnbound

UnboundUnbound
1iphB03UnboundUnboundUnbound

UnboundUnbound
1iphC03UnboundUnboundUnbound

UnboundUnbound
1iphD03UnboundUnboundUnbound

UnboundUnbound
1p7yA03UnboundUnboundUnbound

UnboundUnbound
1p7yB03UnboundUnboundUnbound

UnboundUnbound
1p7yC03UnboundUnboundUnbound

UnboundUnbound
1p7yD03UnboundUnboundUnbound

UnboundUnbound
1p7zA03UnboundUnboundUnbound

UnboundUnbound
1p7zB03UnboundUnboundUnbound

UnboundUnbound
1p7zC03UnboundUnboundUnbound

UnboundUnbound
1p7zD03UnboundUnboundUnbound

UnboundUnbound
1p80A03UnboundUnboundUnbound

UnboundUnbound
1p80B03UnboundUnboundUnbound

UnboundUnbound
1p80C03UnboundUnboundUnbound

UnboundUnbound
1p80D03UnboundUnboundUnbound

UnboundUnbound
1p81A03UnboundUnboundUnbound

UnboundUnbound
1p81B03UnboundUnboundUnbound

UnboundUnbound
1p81C03UnboundUnboundUnbound

UnboundUnbound
1p81D03UnboundUnboundUnbound

UnboundUnbound
1qf7A03UnboundUnboundUnbound

UnboundUnbound
1qf7B03UnboundUnboundUnbound

UnboundUnbound
1qf7C03UnboundUnboundUnbound

UnboundUnbound
1qf7D03UnboundUnboundUnbound

UnboundUnbound
1qwsA03UnboundUnboundUnbound

UnboundUnbound
1qwsB03UnboundUnboundUnbound

UnboundUnbound
1qwsC03UnboundUnboundUnbound

UnboundUnbound
1qwsD03UnboundUnboundUnbound

UnboundUnbound

Active-site residues
resource
Swiss-prot;P21179 & literature [4], [5], [7], [9], [11], [13], [16]
pdbCatalytic residuesCofactor-binding residuescomment
1cf9A01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant V169C
1cf9B01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant V169C
1cf9C01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant V169C
1cf9D01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant V169C
1gg9A01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1gg9B01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1gg9C01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1gg9D01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1ggeA01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1ggeB01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1ggeC01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1ggeD01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1ggfA01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1ggfB01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1ggfC01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1ggfD01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128N
1gghA01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128A
1gghB01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128A
1gghC01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128A
1gghD01       ;ASN 201;HIS 392
TYR 415(Heme binding)
mutant H128A
1ggjA01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201A
1ggjB01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201A
1ggjC01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201A
1ggjD01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201A
1ggkA01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201H
1ggkB01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201H
1ggkC01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201H
1ggkD01HIS 128;       ;HIS 392
TYR 415(Heme binding)
mutant N201H
1iphA01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1iphB01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1iphC01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1iphD01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)

1p7yA01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181A
1p7yB01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181A
1p7yC01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181A
1p7yD01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181A
1p7zA01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181S
1p7zB01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181S
1p7zC01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181S
1p7zD01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181S
1p80A01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181Q
1p80B01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181Q
1p80C01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181Q
1p80D01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181Q
1p81A01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181E
1p81B01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181E
1p81C01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181E
1p81D01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181E
1qf7A01HIS 128;ASN 201;       
TYR 415(Heme binding)
mutant H392Q
1qf7B01HIS 128;ASN 201;       
TYR 415(Heme binding)
mutant H392Q
1qf7C01HIS 128;ASN 201;       
TYR 415(Heme binding)
mutant H392Q
1qf7D01HIS 128;ASN 201;       
TYR 415(Heme binding)
mutant H392Q
1qwsA01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181N
1qwsB01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181N
1qwsC01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181N
1qwsD01HIS 128;ASN 201;HIS 392
TYR 415(Heme binding)
mutant D181N
1cf9A02               


1cf9B02               


1cf9C02               


1cf9D02               


1gg9A02               


1gg9B02               


1gg9C02               


1gg9D02               


1ggeA02               


1ggeB02               


1ggeC02               


1ggeD02               


1ggfA02               


1ggfB02               


1ggfC02               


1ggfD02               


1gghA02               


1gghB02               


1gghC02               


1gghD02               


1ggjA02               


1ggjB02               


1ggjC02               


1ggjD02               


1ggkA02               


1ggkB02               


1ggkC02               


1ggkD02               


1iphA02               


1iphB02               


1iphC02               


1iphD02               


1p7yA02               


1p7yB02               


1p7yC02               


1p7yD02               


1p7zA02               


1p7zB02               


1p7zC02               


1p7zD02               


1p80A02               


1p80B02               


1p80C02               


1p80D02               


1p81A02               


1p81B02               


1p81C02               


1p81D02               


1qf7A02               


1qf7B02               


1qf7C02               


1qf7D02               


1qwsA02               


1qwsB02               


1qwsC02               


1qwsD02               


1cf9A03               


1cf9B03               


1cf9C03               


1cf9D03               


1gg9A03               


1gg9B03               


1gg9C03               


1gg9D03               


1ggeA03               


1ggeB03               


1ggeC03               


1ggeD03               


1ggfA03               


1ggfB03               


1ggfC03               


1ggfD03               


1gghA03               


1gghB03               


1gghC03               


1gghD03               


1ggjA03               


1ggjB03               


1ggjC03               


1ggjD03               


1ggkA03               


1ggkB03               


1ggkC03               


1ggkD03               


1iphA03               


1iphB03               


1iphC03               


1iphD03               


1p7yA03               


1p7yB03               


1p7yC03               


1p7yD03               


1p7zA03               


1p7zB03               


1p7zC03               


1p7zD03               


1p80A03               


1p80B03               


1p80C03               


1p80D03               


1p81A03               


1p81B03               


1p81C03               


1p81D03               


1qf7A03               


1qf7B03               


1qf7C03               


1qf7D03               


1qwsA03               


1qwsB03               


1qwsC03               


1qwsD03               



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]Fig.6, Fig.7, p.1017-1021
[11]Fig.6
[17]


references
[1]
PubMed ID2543292
JournalArch Biochem Biophys
Year1989
Volume271
Pages323-31
AuthorsSchellhorn HE, Pou S, Moody C, Hassan HM
TitleAn electron spin resonance study of oxyradical generation in superoxide dismutase- and catalase-deficient mutants of Escherichia coli K-12.
[2]
PubMed ID2187997
JournalJ Mol Biol
Year1990
Volume213
Pages219-20
AuthorsTormo J, Fita I, Switala J, Loewen PC
TitleCrystallization and preliminary X-ray diffraction analysis of catalase HPII from Escherichia coli.
[3]
PubMed ID1662642
JournalFEBS Lett
Year1991
Volume295
Pages123-6
AuthorsDawson JH, Bracete AM, Huff AM, Kadkhodayan S, Zeitler CM, Sono M, Chang CK, Loewen PC
TitleThe active site structure of E. coli HPII catalase. Evidence favoring coordination of a tyrosinate proximal ligand to the chlorin iron.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID95393020
PubMed ID7663946
JournalStructure
Year1995
Volume3
Pages491-502
AuthorsBravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I
TitleCrystal structure of catalase HPII from Escherichia coli.
Related PDB1iph
Related Swiss-protP21179
[5]
PubMed ID8955627
JournalGene
Year1996
Volume179
Pages39-44
AuthorsLoewen P
TitleProbing the structure of catalase HPII of Escherichia coli--a review.
[6]
PubMed ID8621527
JournalJ Biol Chem
Year1996
Volume271
Pages8863-8
AuthorsMurshudov GN, Grebenko AI, Barynin V, Dauter Z, Wilson KS, Vainshtein BK, Melik-Adamyan W, Bravo J, Ferran JM, Ferrer JC, Switala J, Loewen PC, Fita I
TitleStructure of the heme d of Penicillium vitale and Escherichia coli catalases.
[7]
PubMed ID9185614
JournalArch Biochem Biophys
Year1997
Volume342
Pages58-67
AuthorsObinger C, Maj M, Nicholls P, Loewen P
TitleActivity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase.
[8]
PubMed ID9479449
JournalBiochimie
Year1997
Volume79
Pages667-71
AuthorsJouve HM, Andreoletti P, Gouet P, Hajdu J, Gagnon J
TitleStructural analysis of compound I in hemoproteins: study on Proteus mirabilis catalase.
[9]
PubMed ID9144772
JournalProtein Sci
Year1997
Volume6
Pages1016-23
AuthorsBravo J, Fita I, Ferrer JC, Ens W, Hillar A, Switala J, Loewen PC
TitleIdentification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli.
[10]
PubMed ID9659382
JournalBiochim Biophys Acta
Year1998
Volume1384
Pages209-22
AuthorsMaj M, Loewen P, Nicholls P
TitleE. coli HPII catalase interaction with high spin ligands: formate and fluoride as active site probes.
[11]
CommentsX-ray crystallography
PubMed ID10488114
JournalJ Biol Chem
Year1999
Volume274
Pages27717-25
AuthorsMate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I
TitleMutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.
Related PDB1cf9
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID99190072
PubMed ID10091651
JournalProtein Sci
Year1999
Volume8
Pages490-8
AuthorsSevinc MS, Mate MJ, Switala J, Fita I, Loewen PC
TitleRole of the lateral channel in catalase HPII of Escherichia coli.
Related Swiss-protP21179
[13]
PubMed ID10022351
JournalProteins
Year1999
Volume34
Pages155-66
AuthorsBravo J, Mate MJ, Schneider T, Switala J, Wilson K, Loewen PC, Fita I
TitleStructure of catalase HPII from Escherichia coli at 1.9 A resolution.
[14]
PubMed ID11275470
JournalFree Radic Biol Med
Year2001
Volume30
Pages709-14
AuthorsBrunelli L, Yermilov V, Beckman JS
TitleModulation of catalase peroxidatic and catalatic activity by nitric oxide.
[15]
PubMed ID11119647
JournalProteins
Year2001
Volume42
Pages230-6
AuthorsHorvath MM, Grishin NV
TitleThe C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily.
[16]
CommentsX-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
Medline ID21348730
PubMed ID11455600
JournalProteins
Year2001
Volume44
Pages270-81
AuthorsMelik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC
TitleSubstrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli.
Related PDB1gg9,1gge,1ggf,1ggh,1ggj,1ggk,1qf7
Related Swiss-protP21179
[17]
CommentsX-ray crystallography
PubMed ID12777389
JournalJ Biol Chem
Year2003
Volume278
Pages31290-6
AuthorsChelikani P, Carpena X, Fita I, Loewen PC
TitleAn electrical potential in the access channel of catalases enhances catalysis.
Related PDB1p7y,1p7z,1p80,1p81,1qws
[18]
PubMed ID14745498
JournalCell Mol Life Sci
Year2004
Volume61
Pages192-208
AuthorsChelikani P, Fita I, Loewen PC
TitleDiversity of structures and properties among catalases.

comments
There are three types of catalases, which are monofunctional catalases, bifunctional catalase-peroxidases and manganese-containing catalases. This enzyme corresponds to monofunctional catalases.
This enzyme catalyzes the following reactions:
(1) Enzyme(Por-Fe(III)) + H2O2 -> Compound I(Por(+)-Fe(IV)=O) + H2O
(2) Compound I(Por(+)-Fe(IV)=O) + H2O2 -> Enzyme(Por-Fe(III)) + H2O + O2
During catalysis, a covalent bond between the ND o the imidazole ring of His392 and the CB of Tyr415 is formed, according to the literature [9]. Moreover, heme group also self-catalyzes to facilitate spirolactone cyclization (see [9]).

createdupdated
2005-05-192009-02-26


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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