EzCatDB T00021

Murshudov 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

Title

Structure of the heme d of Penicillium vitale and Escherichia coli catalases.

[7]

PubMed ID

9185614

Journal

Arch Biochem Biophys

Year

1997

Volume

342

Pages

58-67

Authors

Obinger C, Maj M, Nicholls P, Loewen P

Title

Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase.

[8]

PubMed ID

9479449

Journal

Biochimie

Year

1997

Volume

Pages

667-71

Authors

Jouve HM, Andreoletti P, Gouet P, Hajdu J, Gagnon J

Title

Structural analysis of compound I in hemoproteins: study on Proteus mirabilis catalase.

[9]

PubMed ID

9144772

Journal

Protein Sci

Year

1997

Volume

Pages

1016-23

Authors

Bravo J, Fita I, Ferrer JC, Ens W, Hillar A, Switala J, Loewen PC

Title

Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli.

[10]

PubMed ID

9659382

Journal

Biochim Biophys Acta

Year

1998

Volume

1384

Pages

209-22

Authors

Maj M, Loewen P, Nicholls P

Title

E. coli HPII catalase interaction with high spin ligands: formate and fluoride as active site probes.

[11]

Comments

X-ray crystallography

PubMed ID

10488114

Journal

J Biol Chem

Year

1999

Volume

274

Pages

27717-25

Authors

Mate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I

Title

Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.

Related PDB

1cf9

[12]

Comments

X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Medline ID

99190072

PubMed ID

10091651

Journal

Protein Sci

Year

1999

Volume

Pages

490-8

Authors

Sevinc MS, Mate MJ, Switala J, Fita I, Loewen PC

Title

Role of the lateral channel in catalase HPII of Escherichia coli.

Related UniProtKB

P21179

[13]

PubMed ID

10022351

Journal

Proteins

Year

1999

Volume

Pages

155-66

Authors

Bravo J, Mate MJ, Schneider T, Switala J, Wilson K, Loewen PC, Fita I

Title

Structure of catalase HPII from Escherichia coli at 1.9 A resolution.

[14]

PubMed ID

11275470

Journal

Free Radic Biol Med

Year

2001

Volume

Pages

709-14

Authors

Brunelli L, Yermilov V, Beckman JS

Title

Modulation of catalase peroxidatic and catalatic activity by nitric oxide.

[15]

PubMed ID

11119647

Journal

Proteins

Year

2001

Volume

Pages

230-6

Authors

Horvath MM, Grishin NV

Title

The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily.

[16]

Comments

X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).

Medline ID

21348730

PubMed ID

11455600

Journal

Proteins

Year

2001

Volume

Pages

270-81

Authors

Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC

Title

Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli.

Related PDB

1gg9,1gge,1ggf,1ggh,1ggj,1ggk,1qf7

Related UniProtKB

P21179

[17]

Comments

X-ray crystallography

PubMed ID

12777389

Journal

J Biol Chem

Year

2003

Volume

278

Pages

31290-6

Authors

Chelikani P, Carpena X, Fita I, Loewen PC

Title

An electrical potential in the access channel of catalases enhances catalysis.

Related PDB

1p7y,1p7z,1p80,1p81,1qws

[18]

PubMed ID

14745498

Journal

Cell Mol Life Sci

Year

2004

Volume

Pages

192-208

Authors

Chelikani P, Fita I, Loewen PC

Title

Diversity 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]).

created

updated

2005-05-19

2009-02-26

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 2008)
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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )