Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

Reference on EC 4.2.1.40 - glucarate dehydratase and Organism(s) Escherichia coli and UniProt Accession P0AES2

Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marsh, C.A.
An enzymatic determination of D-glucaric acid by conversion to pyruvate
Anal. Biochem.
145
266-272
1985
Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Blumenthal, H.J.
D-glucarate dehydratase
Methods Enzymol.
9
660-665
1966
Bacillus subtilis, Citrobacter freundii, Escherichia coli, Klebsiella aerogenes, Klebsiella pneumoniae, Paracolobactrum sp., Pectobacterium carotovorum, Priestia megaterium
-
Manually annotated by BRENDA team
Gulick, A.M.; Hubbard, B.K.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli
Biochemistry
39
4590-4602
2000
Escherichia coli (P0AES2), Escherichia coli
Manually annotated by BRENDA team
Gulick, A.M.; Hubbard, B.K.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli
Biochemistry
40
10054-10062
2001
Escherichia coli (P0AES2), Escherichia coli
Manually annotated by BRENDA team