Enzymes
| UniProtKB help_outline | 2,014 proteins |
| Enzyme class help_outline |
|
| GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline maleate Identifier CHEBI:30780 Charge -2 Formula C4H2O4 InChIKeyhelp_outline VZCYOOQTPOCHFL-UPHRSURJSA-L SMILEShelp_outline [O-]C(=O)\C=C/C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline fumarate Identifier CHEBI:29806 (CAS: 142-42-7) help_outline Charge -2 Formula C4H2O4 InChIKeyhelp_outline VZCYOOQTPOCHFL-OWOJBTEDSA-L SMILEShelp_outline [O-]C(=O)\C=C\C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 41 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13169 | RHEA:13170 | RHEA:13171 | RHEA:13172 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase.
Fisch F., Fleites C.M., Delenne M., Baudendistel N., Hauer B., Turkenburg J.P., Hart S., Bruce N.C., Grogan G.
Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have reveal ... >> More
Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate. << Less
J. Am. Chem. Soc. 132:11455-11457(2010) [PubMed] [EuropePMC]
-
Gene cloning and characterization of maleate cis-trans isomerase from Alcaligenes faecalis.
Hatakeyama K., Asai Y., Uchida Y., Kobayashi M., Terasawa M., Yukawa H.
Maleate cis-trans isomerase, which catalyses the conversion of maleate to fumarate, was purified and characterized from Alcaligenes faecalis IFO13111. The molecular weight of maleate isomerase was estimated as 60 kDa, consisting of a 28 kDa dimer as shown by gel-filtration chromatography and SDS-P ... >> More
Maleate cis-trans isomerase, which catalyses the conversion of maleate to fumarate, was purified and characterized from Alcaligenes faecalis IFO13111. The molecular weight of maleate isomerase was estimated as 60 kDa, consisting of a 28 kDa dimer as shown by gel-filtration chromatography and SDS-PAGE analysis. Kinetic studies showed that the Michaelis constant for maleate was 4.0 x 10(-5) M. The reverse reaction (fumarate to maleate) activity of the enzyme was detected even though it was quite weak. The maleate isomerase gene (maiA) was cloned by hybridization using the oligonucleotide DNA probes designed on the basis of the determined N-terminal amino acid sequences of the purified enzyme. The determined DNA sequence of the maiA gene contains an open reading frame which encodes a 254-amino-acid sequence. The amino acid sequence of the maiA gene product shows no significant homology to any amino acid sequences in the protein data base. << Less
Biochem. Biophys. Res. Commun. 239:74-79(1997) [PubMed] [EuropePMC]