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Sequence of CATC_PSEPU

EC Number:5.3.3.4

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
muconolactone DELTA-isomerase
P00948
Pseudomonas putida
96
11116
Reaction
(+)-muconolactone = (4,5-dihydro-5-oxofuran-2-yl)-acetate
Other sequences found for EC No. 5.3.3.4

General information:

Sequence
 0 MLFHVKMTVK LPVDMDPAKA TQLKADEKEL AQRLQREGTW RHLWRIAGHY ANYSVFDVSS
60 VEACNDTLMQ LPLFPYMDIE VDGLCRHPSS IHSDDR
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1037814
Aldrich T.L.,Chakrabarty A.M.
Transcriptional regulation, nucleotide sequence, and localization of the promoter of the catBC operon in Pseudomonas putida.
J. Bacteriol.
170
1297-1304
1988
1037815
Houghton J.E.,Brown T.M.,Appel A.J.,Hughes E.J.,Ornston L.N.
Discontinuities in the evolution of Pseudomonas putida cat genes.
J. Bacteriol.
177
401-412
1995
1037816
McCorkle G.M.,Yeh W.-K.,Fletcher P.,Ornston L.N.
Repetitions in the NH2-terminal amino acid sequence of beta-ketoadipate enol-lactone hydrolase from Pseudomonas putida.
J. Biol. Chem.
255
6335-6341
1980
1037817
Meagher R.B.
Purification and partial amino acid sequence of the cyanogen bromide fragments of muconolactone isomerase from Pseudomonas putida.
Biochim. Biophys. Acta
494
33-47
1977
1037818
Ornston L.N.
The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway.
J. Biol. Chem.
241
3795-3799
1966
1037819
Katti S.K.,Katz B.A.,Wyckoff H.W.
Crystal structure of muconolactone isomerase at 3.3-A resolution.
J. Mol. Biol.
205
557-571
1989