scholarly article | Q13442814 |
P356 | DOI | 10.1016/S0969-2126(99)80122-1 |
P698 | PubMed publication ID | 10467151 |
P2093 | author name string | M Fukuda | |
Y Mitsui | |||
E Masai | |||
K Sugimoto | |||
T Senda | |||
H Aoshima | |||
P2860 | cites work | Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution | Q27730790 |
Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102 | Q27732711 | ||
Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site | Q27741647 | ||
Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding | Q27741668 | ||
Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate | Q27743339 | ||
The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates | Q27748882 | ||
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures | Q27860894 | ||
Automated refinement of protein models | Q27860928 | ||
Refinement of macromolecular structures by the maximum-likelihood method | Q27861011 | ||
The CCP4 suite: programs for protein crystallography | Q27861090 | ||
Molecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilis | Q28330942 | ||
Conformation of Polypeptides and Proteins | Q29617878 | ||
Structure and assembly of protocatechuate 3,4-dioxygenase | Q30196085 | ||
Functional and evolutionary relationships among diverse oxygenases | Q33972461 | ||
Evolutionary relationships among extradiol dioxygenases | Q35614251 | ||
A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: cloning and characterization of the hpp operon | Q35631054 | ||
Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases | Q36812919 | ||
Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10. | Q39846665 | ||
Nucleotide sequence of metapyrocatechase I (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222. | Q40517338 | ||
Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity. | Q52308271 | ||
X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism | Q57943724 | ||
PROCHECK: a program to check the stereochemical quality of protein structures | Q26778411 | ||
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures | Q26778412 | ||
Processing of X-ray diffraction data collected in oscillation mode | Q26778468 | ||
An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2 | Q27618597 | ||
Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad | Q27729302 | ||
P433 | issue | 8 | |
P921 | main subject | crystal structure | Q895901 |
P304 | page(s) | 953-65 | |
P577 | publication date | 1999-08-15 | |
P1433 | published in | Structure | Q15709970 |
P1476 | title | Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions | |
P478 | volume | 7 |
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