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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
5.2.1.1
748863
Computational investigations on the catalytic mechanism of maleate isomerase the role of the active site cysteine residues
Phys. Chem. Chem. Phys.
16
12462-12474
2014
Nocardia farcinica
24827730
5.2.1.1
748863
Computational investigations on the catalytic mechanism of maleate isomerase the role of the active site cysteine residues
Phys. Chem. Chem. Phys.
16
12462-12474
2014
Nocardia farcinica IFM 10152
24827730
5.2.1.1
715258
A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase
J. Am. Chem. Soc.
132
11455-11457
2010
Nocardia farcinica
20677745
5.2.1.1
715258
A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase
J. Am. Chem. Soc.
132
11455-11457
2010
Nocardia farcinica IFM 10152
20677745
5.2.1.1
650608
Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens
Biosci. Biotechnol. Biochem.
64
1477-1485
2000
Alcaligenes faecalis
10945267
5.2.1.1
650608
Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens
Biosci. Biotechnol. Biochem.
64
1477-1485
2000
Geobacillus stearothermophilus
10945267
5.2.1.1
650608
Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens
Biosci. Biotechnol. Biochem.
64
1477-1485
2000
Serratia marcescens
10945267
5.2.1.1
650608
Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens
Biosci. Biotechnol. Biochem.
64
1477-1485
2000
Serratia marcescens IFO3736
10945267
5.2.1.1
2451
cis-trans Isomerization
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
381-406
1972
Alcaligenes faecalis
-
5.2.1.1
2451
cis-trans Isomerization
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
381-406
1972
Pseudomonas sp.
-
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