Pathways & interactions
Literature: Intradiol ring-cleavage dioxygenase, C-terminal (IPR000627)
References used in this entry
The following publications were referred to in the abstract:
Essays Biochem. 34 173-89 1999
PMID: 10730195 Related citations
Crystal structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing gram-positive Rhodococcus opacus 1CP.
Ferraroni M, Solyanikova IP, Kolomytseva MP, Scozzafava A, Golovleva L, Briganti F.
J. Biol. Chem. 279 27646-55 2004
PMID: 15060064 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Bacterial aromatic ring-cleavage enzymes are classified into two different gene families.
Harayama S, Rekik M.
J. Biol. Chem. 264 15328-33 1989
PMID: 2670937 Related citations
Structure and assembly of protocatechuate 3,4-dioxygenase.
Ohlendorf DH, Lipscomb JD, Weber PC.
Nature 336 403-5 1988
PMID: 3194022 Related citations
The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
Vetting MW, Ohlendorf DH.
Structure 8 429-40 2000
PMID: 10801478 Related citations
Structure of Acinetobacter strain ADP1 protocatechuate 3, 4-dioxygenase at 2.2 A resolution: implications for the mechanism of an intradiol dioxygenase.
Vetting MW, D'Argenio DA, Ornston LN, Ohlendorf DH.
Biochemistry 39 7943-55 2000
PMID: 10891075 Related citations
Roles of the equatorial tyrosyl iron ligand of protocatechuate 3,4-dioxygenase in catalysis.
Valley MP, Brown CK, Burk DL, Vetting MW, Ohlendorf DH, Lipscomb JD.
Biochemistry 44 11024-39 2005
PMID: 16101286 Related citations
Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.
Brown CK, Vetting MW, Earhart CA, Ohlendorf DH.
Annu. Rev. Microbiol. 58 555-85 2004
PMID: 15487948 Related citations