Reference on EC 4.2.1.40 - glucarate dehydratase and Organism(s) Pseudomonas putida and UniProt Accession P42206
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AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hubbard, B.K.; Koch, M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli
Biochemistry
37
14369-14375
1998
Bacillus subtilis, Escherichia coli, Pseudomonas putida
Palmer, D.R.J.; Wieczorek, S.J.; Hubbard, B.K.; Mrachko, G.T.; Gerit, J.A.
Importance of mechanistic imperatives in enzyme-catalyzed beta-elimination reactions: stereochemical consequences of the dehydration reaction catalyzed by D-galactonate dehydratase from Escherichia coli and D-glucarate dehydratase from Pseudomonas putida
J. Am. Chem. Soc.
199
9580-9581
1997
Pseudomonas putida
-
Palmer, D.R.J.; Gerit, J.A.
Evolution of enzymatic activities: multiple pathways for generating and partitioning a common enolic intermediate by glucarate dehydratase from Pseudomonas putida
J. Am. Chem. Soc.
118
10323-10342
1996
Pseudomonas putida
-
Palmer, D.R.J.; Hubbard, B.K.; Gerit, J.A.
Evolution of enzymatic activities in the enolase superfamily: partitioning of reactive intermediates by (D)-glucarate dehydratase from Pseudomonas putida
Biochemistry
37
14350-14357
1998
Pseudomonas putida
Gulick, A.M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida
Biochemistry
37
14358-14368
1998
Pseudomonas putida (P42206), Pseudomonas putida
