EzCatDB: D00446

DB codeD00446
CATH domainDomain 13.10.180.10
Domain 23.10.180.10Catalytic domain
E.C.1.13.11.2
CSA1mpy
MACiEM0034

CATH domainRelated DB codes (homologues)
3.10.180.10D00447,D00448,S00540,S00185

Enzyme Name
Swiss-protKEGG

P06622
Protein nameMetapyrocatechasecatechol 2,3-dioxygenase
2,3-pyrocatechase
catechol 2,3-oxygenase
catechol oxygenase
metapyrocatechase
pyrocatechol 2,3-dioxygenase
SynonymsMPC
EC 1.13.11.2
CatO2ase
Catechol 2,3-dioxygenase

KEGG pathways
MAP codePathways
MAP00362Benzoate degradation via hydroxylation
MAP00622Toluene and xylene degradation
MAP006271,4-Dichlorobenzene degradation
MAP00629Carbazole degradation
MAP00643Styrene degradation

Swiss-prot:Accession NumberP06622
Entry nameXYLE1_PSEPU
ActivityCatechol + O(2) = 2-hydroxymuconate semialdehyde.
SubunitHomotetramer.
Subcellular location
CofactorFe(2+) ion.


CofactorsSubstratesProducts
KEGG-idC00023C00090C00007C00682
CompoundIronCatecholO22-Hydroxymuconate semialdehyde
Typeheavy metalaromatic ring (only carbon atom)otherscarbohydrate,carboxyl group
1mpyA01UnboundUnboundUnboundUnbound
1mpyB01UnboundUnboundUnboundUnbound
1mpyC01UnboundUnboundUnboundUnbound
1mpyD01UnboundUnboundUnboundUnbound
1mpyA02Bound:FE2UnboundUnboundUnbound
1mpyB02Bound:FE2UnboundUnboundUnbound
1mpyC02Bound:FE2UnboundUnboundUnbound
1mpyD02Bound:FE2UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P06622 & literature [14]
pdbCatalytic residuesCofactor-binding residues
1mpyA01

1mpyB01

1mpyC01

1mpyD01

1mpyA02HIS 199
HIS 153;HIS 214;GLU 265(Iron binding)
1mpyB02HIS 199
HIS 153;HIS 214;GLU 265(Iron binding)
1mpyC02HIS 199
HIS 153;HIS 214;GLU 265(Iorn binding)
1mpyD02HIS 199
HIS 153;HIS 214;GLU 265(Iron binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[10]Fig.7, p.6656-66574
[11]

[14]Fig.1, p.32

references
[1]
PubMed ID6245930
JournalFEBS Lett
Year1980
Volume112
Pages83-5
AuthorsTatsuno Y, Saeki Y, Nozaki M, Otsuka S, Maeda Y
TitleMossbauer spectra of metapyrocatechase.
[2]
PubMed ID6773944
JournalJ Biol Chem
Year1980
Volume255
Pages8465-71
AuthorsSaeki Y, Nozaki M, Senoh S
TitleCleavage of pyrogallol by non-heme iron-containing dioxygenases.
[3]
PubMed ID2997190
JournalJ Biol Chem
Year1985
Volume260
Pages14035-44
AuthorsArciero DM, Orville AM, Lipscomb JD
Title17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases.
[4]
PubMed ID3015028
JournalArch Biochem Biophys
Year1986
Volume248
Pages130-7
AuthorsPascal RA Jr, Huang DS
TitleReactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases.
[5]
PubMed ID3365096
JournalArch Microbiol
Year1988
Volume149
Pages188-97
AuthorsEngesser KH, Cain RB, Knackmuss HJ
TitleBacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657.
[6]
PubMed ID8075079
JournalBiochemistry
Year1994
Volume33
Pages10777-84
AuthorsBertini I, Briganti F, Mangani S, Nolting HF, Scozzafava A
TitleX-ray absorption studies on catechol 2,3-dioxygenase from Pseudomonas putida mt2.
[7]
PubMed ID8163017
JournalFEBS Lett
Year1994
Volume343
Pages56-60
AuthorsBertini I, Briganti F, Scozzafava A
TitleAliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2.
[8]
PubMed ID8180697
JournalMicrobiology
Year1994
Volume140
Pages321-30
AuthorsCandidus S, van Pee KH, Lingens F
TitleThe catechol 2,3-dioxygenase gene of Rhodococcus rhodochrous CTM: nucleotide sequence, comparison with isofunctional dioxygenases and evidence for an active-site histidine.
[9]
PubMed ID7710322
JournalArch Microbiol
Year1995
Volume163
Pages65-9
AuthorsWinkler J, Eltis LD, Dwyer DF, Rohde M
TitleTetrameric structure and cellular location of catechol 2,3-dioxygenase.
[10]
PubMed ID7756296
JournalBiochemistry
Year1995
Volume34
Pages6649-59
AuthorsShu L, Chiou YM, Orville AM, Miller MA, Lipscomb JD, Que L Jr
TitleX-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism.
[11]
PubMed ID9056848
JournalBiochem Soc Trans
Year1997
Volume25
Pages81-5
AuthorsBugg TD, Sanvoisin J, Spence EL
TitleExploring the catalytic mechanism of the extradiol catechol dioxygenases.
[12]
PubMed ID9276689
JournalJ Biochem (Tokyo)
Year1997
Volume122
Pages201-4
AuthorsKita A, Kita S, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K
TitleCrystallization and preliminary X-ray diffraction studies of expressed Pseudomonas putida catechol 2,3-dioxygenase.
[13]
PubMed ID9545294
JournalJ Biol Chem
Year1998
Volume273
Pages9622-9
AuthorsHugo N, Armengaud J, Gaillard J, Timmis KN, Jouanneau Y
TitleA novel -2Fe-2S- ferredoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechol 2,3-dioxygenase.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID99148110
PubMed ID10368270
JournalStructure Fold Des
Year1999
Volume7
Pages25-34
AuthorsKita A, Kita S, Fujisawa I, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K
TitleAn archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2.
Related PDB1mpy
Related Swiss-protP06622
[15]
PubMed ID11565853
JournalJ Biomol Struct Dyn
Year2001
Volume19
Pages75-83
AuthorsDai L, Ji C, Gao D, Wang J, Jiang T, Bi A, Sheng X, Mao Y
TitleModeling and analysis of the structure of the thermostable catechol 2,3-dioxygenase from Bacillus Stearothermophilus.
[16]
PubMed ID12519074
JournalBiochem J
Year2003
Volume371
Pages557-64
AuthorsOkuta A, Ohnishi K, Yagame S, Harayama S
TitleIntersubunit interaction and catalytic activity of catechol 2,3-dioxygenases.
[17]
PubMed ID14769058
JournalJ Biomol Struct Dyn
Year2004
Volume21
Pages657-62
AuthorsZhang JH, Zhang LL, Zhou LX
TitleThermostability of protein studied by molecular dynamics simulation.


createdupdated
2004-10-282009-03-16
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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