We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
maleate cis-trans isomerase, maleate isomerase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Isomerase, maleate
-
-
-
-
maleate cis-trans isomerase
-
MaiA
-
Pp-Iso
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Maleate = fumarate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cis-trans-isomerization
-
cis-trans-isomerization
-
-
double bond
-
cis-trans-isomerization
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
maleate cis-trans-isomerase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
?
-
Maleate
Fumarate
-
-
-
?
Maleate
Fumarate
-
reverse reaction is not observed
-
?
Maleate
Fumarate
-
r, reverse reaction is quite weak
-
?
Maleate
Fumarate
-
-
-
ir
Maleate
Fumarate
-
-
-
ir
Maleate
Fumarate
-
reverse reaction is not observed
-
?
Maleate
Fumarate
Asn17 and Asn169 play critical roles in recognizing maleate
-
-
r
Maleate
Fumarate
Asn17 and Asn169 play critical roles in recognizing maleate
-
-
r
Maleate
Fumarate
whole cells of recombinant Escherichia coli expressing enzyme mutant MaiR-D48 catalyze the isomerization of maleic acid to fumaric acid at 1 M substrate concentration
-
-
r
additional information
?
-
-
enzyme is induced by malonate favorably in a poor medium whereas it is repressed in a rich medium by carbon sources such as intermediates of the tricarboxylic acid cycle, catabolite repression is reversed by minimizing the functioning of the tricarboxylic acid cycle
-
-
?
additional information
?
-
-
malonate and ketomalonate are more effective than maleate in inducing isomerase synthesis
-
-
?
additional information
?
-
-
induction by tartronate, ketomalonate and ethylmalonate. Repression by oxalacetate or DL-malate
-
-
?
additional information
?
-
-
enzyme is induced by malonate favorably in a poor medium whereas it is repressed in a rich medium by carbon sources such as intermediates of the tricarboxylic acid cycle, catabolite repression is reversed by minimizing the functioning of the tricarboxylic acid cycle
-
-
?
additional information
?
-
-
induction by tartronate, ketomalonate and ethylmalonate. Repression by oxalacetate or DL-malate
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
residue Cys194, upon activation via the substrate, acts as a nucleophile and Cys76 acts as an acid/base catalyst, forming a succinyl-Cys intermediate in a concerted fashion. The mechanism proceeds via multiple steps by substrate rotation around C2-C3 with the assistance of the now negatively charged Cys76, leading to the formation of fumarate
-
-
?
additional information
?
-
residue Cys194, upon activation via the substrate, acts as a nucleophile and Cys76 acts as an acid/base catalyst, forming a succinyl-Cys intermediate in a concerted fashion. The mechanism proceeds via multiple steps by substrate rotation around C2-C3 with the assistance of the now negatively charged Cys76, leading to the formation of fumarate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
?
-
Maleate
Fumarate
-
-
-
r
Maleate
Fumarate
whole cells of recombinant Escherichia coli expressing enzyme mutant MaiR-D48 catalyze the isomerization of maleic acid to fumaric acid at 1 M substrate concentration
-
-
r
additional information
?
-
-
enzyme is induced by malonate favorably in a poor medium whereas it is repressed in a rich medium by carbon sources such as intermediates of the tricarboxylic acid cycle, catabolite repression is reversed by minimizing the functioning of the tricarboxylic acid cycle
-
-
?
additional information
?
-
-
malonate and ketomalonate are more effective than maleate in inducing isomerase synthesis
-
-
?
additional information
?
-
-
induction by tartronate, ketomalonate and ethylmalonate. Repression by oxalacetate or DL-malate
-
-
?
additional information
?
-
-
enzyme is induced by malonate favorably in a poor medium whereas it is repressed in a rich medium by carbon sources such as intermediates of the tricarboxylic acid cycle, catabolite repression is reversed by minimizing the functioning of the tricarboxylic acid cycle
-
-
?
additional information
?
-
-
induction by tartronate, ketomalonate and ethylmalonate. Repression by oxalacetate or DL-malate
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CO2
-
increases activity by 20-30%
Fe2+
-
increases activity by 20-30%
Mn2+
-
increases activity by 20-30%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
bromomaleate
weak inhibitor
NaCN
-
0.6 mM, 20% inhibition
NaF
-
0.6-3 mM, 18-45% inhibition
p-chloromercuriphenylsulfonate
-
-
p-Substituted mercuribenzoate
p-toluenesulfonchloramide
-
1 mM, complete inhibition
Semicarbazide
-
1 mM, weak inhibition
Bromoacetate
-
-
cyanide
-
1 mM, weak inhibition
cyanide
-
KCN, 1 mM, 20% inhibition
EDTA
-
-
EDTA
-
1 mM, 7% inhibition
EDTA
-
0.1 mM, 20% inhibition
H2O2
-
-
H2O2
-
1 mM, complete inhibition, Met201 is one of the targeted sites for the inactivation by chemical oxidation
iodoacetamide
-
-
iodoacetamide
-
1 mM, 72% inhibition
iodoacetate
-
-
iodoacetate
-
1 mM 73% inhibition
iodoacetate
-
0.01 mM, complete inhibition
N-bromosuccinimide
-
1 mM, weak inhibition
N-bromosuccinimide
-
1 mM, complete inhibition
N-Chlorosuccinimide
-
-
N-Chlorosuccinimide
-
1 mM, complete inhibition
p-Substituted mercuribenzoate
-
-
p-Substituted mercuribenzoate
-
0.01 mM, complete inhibition
PCMB
-
0.1 mM, complete inhibition; inhibition is overcome by the addition of sulfhydryl compounds
PCMB
-
0.1 mM, complete inhibition
Sodium periodate
-
-
Sodium periodate
-
1 mM, complete inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dithiothreitol
-
activates
2-mercaptoethanol
-
-
2-mercaptoethanol
-
enhances activity
mercaptans
-
-
-
mercaptans
-
required for activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00053
Maleate
mutant enzyme Y133F, at pH 7.5, temperature not specified in the publication
0.0037
Maleate
mutant enzyme C76S, at pH 7.5, temperature not specified in the publication
0.0046
Maleate
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.007
Maleate
mutant enzyme C194S, at pH 7.5, temperature not specified in the publication
0.1496
Maleate
pH 8.0, 40°C, recombinant enzyme mutant MaiR-D48/49-304AA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00035
Maleate
mutant enzyme C194S, at pH 7.5, temperature not specified in the publication
0.0019
Maleate
mutant enzyme C76S, at pH 7.5, temperature not specified in the publication
0.32
Maleate
mutant enzyme Y133F, at pH 7.5, temperature not specified in the publication
2.8
Maleate
wild type enzyme, at pH 7.5, temperature not specified in the publication
96.7
Maleate
pH 8.0, 40°C, recombinant enzyme mutant MaiR-D48/49-304AA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.05
Maleate
mutant enzyme C194S, at pH 7.5, temperature not specified in the publication
0.513
Maleate
mutant enzyme C76S, at pH 7.5, temperature not specified in the publication
600
Maleate
mutant enzyme Y133F, at pH 7.5, temperature not specified in the publication
610
Maleate
wild type enzyme, at pH 7.5, temperature not specified in the publication
650
Maleate
pH 8.0, 40°C, recombinant enzyme mutant MaiR-D48/49-304AA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.001
bromomaleate
pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
106.8
purified enzyme mutant MaiR-D48/49-304AA, pH 8.0, 40°C
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8
-
-
8
recombinant mutant MaiR-D48/49-304AA
8.4
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 9
activity range, recombinant mutant MaiR-D48/49-304AA
6.5 - 9.3
-
about 50% of maximal activity at pH 6.5 and at pH 9.3
6.8 - 9.3
-
about 50% of maximal activity at pH 6.8 and 9.3
7 - 9
-
more than 75% of maximal activity at pH 7.0 and pH 9.0
7 - 9.3
-
pH 7: about 60% of maximal activity, pH 9.3: about 40% of maximal activity
6.7 - 9.4
-
-
6.7 - 9.4
-
about 50% of maximal activity at pH 6.7 and pH 9.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40
recombinant mutant MaiR-D48/49-304AA
45
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
25 - 60
activity range, recombinant mutant MaiR-D48/49-304AA
30 - 70
-
increase of activity from 30°C to 70°C
35 - 50
-
about 50% of maximal activity at 35°C and 50°C
30 - 60
-
30°C: about 60% of maximal activity, 60°C: about 40% of maximal activity
30 - 60
-
30°C: about 70% of maximal activity, 60°C: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IB-14
-
-
brenda
T501
-
-
brenda
T501
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
gene ro00478
UniProt
brenda
IFO3736
-
-
brenda
IFO3736
-
-
brenda
-
-
-
brenda
IB-14
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
maleate isomerase catalyses the last step in nicotine degradation, the cis-trans isomerization of maleate to fumarate
metabolism
-
maleate isomerase catalyses the last step in nicotine degradation, the cis-trans isomerization of maleate to fumarate
-
additional information
residues C84 and C200 are essential for catalysis, active site structure, overview. The beta2-alpha2 loop and the beta6-alpha7 loop of Pp-Iso have a breathing motion revealed by the molecular dynamics simulation
additional information
-
residues C84 and C200 are essential for catalysis, active site structure, overview. The beta2-alpha2 loop and the beta6-alpha7 loop of Pp-Iso have a breathing motion revealed by the molecular dynamics simulation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
100000
-
gel filtration, sedimentation velocity studies
26950
-
x * 26950, calculation from nucleotide sequence
27971
-
2 * 27971, calculation from nucleotide sequence
28000
-
2 * 28000, SDS-PAGE
28000
-
x * 28000, SDS-PAGE
74000
-
sedimentation velocity experiments
74000
-
sedimentation velocity experiments
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 28000, SDS-PAGE
?
-
x * 26950, calculation from nucleotide sequence
?
-
x * 28000, SDS-PAGE
-
?
-
x * 26950, calculation from nucleotide sequence
-
dimer
-
2 * 28000, SDS-PAGE
dimer
-
2 * 27971, calculation from nucleotide sequence
dimer
dynamic light scattering
dimer
-
dynamic light scattering
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
purified recombinant wild-type alone, and mutant enzyme C200A in complex with substrate maleate, hanging-drop vapour-diffusion method, mixing of 15-20 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 2 mM DTT, with a reservoir solution containing 25% w/v PEG3,350 and 0.1 M Tris, pH 8.5, for the substrate-enzyme mutant complex, and 1.4 M (NH4)2SO4, 120 mM NaCl, and 0.1 M HEPES, pH 7.5, for the free wild-type enzyme, 14°C, X-ray diffraction structure determination and analysis at 2.95 A and 2.10 A resolution, respectively
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C194S
the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
C76S
the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
Y133F
the mutant shows decreased turnover and Km, but about wild type catalytic efficiency
C194S
-
the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
-
C76S
-
the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
-
Y133F
-
the mutant shows decreased turnover and Km, but about wild type catalytic efficiency
-
C200A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, substrate-binding structure: maleate can be found to exist inside a cavity of the enzyme, totally surrounded by the protein
C84A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
C200A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, substrate-binding structure: maleate can be found to exist inside a cavity of the enzyme, totally surrounded by the protein
-
C84A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
M138C
-
mutant enzyme shows 90% of the activity of the wild-type enzyme
M18C
-
mutant enzyme shows 30% of the activity of the wild-type enzyme
M201C
-
mutant enzyme shows 90% of the activity of the wild-type enzyme
M46C
-
mutant enzyme shows 30% of the activity of the wild-type enzyme
M57C
-
mutant enzyme shows 40% of the activity of the wild-type enzyme
M85C
-
mutant enzyme shows 90% of the activity of the wild-type enzyme
M138C
-
mutant enzyme shows 90% of the activity of the wild-type enzyme
-
M18C
-
mutant enzyme shows 30% of the activity of the wild-type enzyme
-
M46C
-
mutant enzyme shows 30% of the activity of the wild-type enzyme
-
M57C
-
mutant enzyme shows 40% of the activity of the wild-type enzyme
-
M85C
-
mutant enzyme shows 90% of the activity of the wild-type enzyme
-
additional information
generation of three catalytically active mutants MaiR-D41/42-304AA, MaiR-D48/49-304AA and MaiR-D52/53-304AA without the hydrophilic and hydrophobic clusters
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 7
-
30°C, rapid loss of activity below pH 5 and above pH 7
2451
5 - 7
-
stable over this range in presence of dithiothreitol for a few weeks. In absence of dithiothreitol the activity is markedly decreased, especially in the alkaline region
2453
6
-
0°C-25°C, maximal stability in presence of small quantities of dithiothreitol
2451
6
-
most stable in acetate buffer at this pH
2453
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0 - 25
-
pH 6, maximal stability in presence of small quantities of dithiothreitol
30
-
15 min, stable below
45
-
30 min, about 10% loss of activity
53
-
30 min, complete inactivation
55 - 60
purified recombinant mutant MaiR-D48/49-304AA, 30 min, over 95% activity at 55°C and about 50% activity at 60°C remaining
57
-
30 min, stable below
40
-
15 min, about 25% loss of activity
40
purified recombinant mutant MaiR-D48/49-304AA, 30 min, completely stable
50
-
15 min, complete loss of activity
50
-
30 min, about 45% loss of activity
60
-
30 min, about 25% loss of activity
60
-
30 min, retains almost 60% of the initial activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
crystallization can be accompanied by a 50% loss in activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme mutant MaiR-D48 shows high oxidative stability
728167
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-20°C, overnight, 10% loss of activity
-
4°C, 20% glycerol, 10 mM thioglycerol, 3 months, 70% loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
recombinant mutant MaiR-D48/49-304AA 2.7fold from Escherichia coli strain Rosetta 2 (DE3) by ammonium sulfate fractionation, anion exchange chromatography, ultratfiltration, and gel filtration
recombinant N- and C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli
-
gene ro00478, recombinant expression of wild-type and mutants in Escherichia coli Rosetta2 (DE3) pLysS
overexpression of N- and C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
synthesis
whole cells of Escherichia coli expressing the enzyme mutant MaiR-D48 catalyze the isomerization of maleic acid to fumaric acid at 1 M substrate concentration showing its potential for industrial use
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kimura, T.; Kawabata, Y.; Sato, E.
Enzymatic production of L-malate from maleate by Alcaligenes sp.
Agric. Biol. Chem.
50
89-94
1986
Alcaligenes sp., Alcaligenes sp. T501
-
brenda
Seltzer, S.
cis-trans Isomerization
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
381-406
1972
Alcaligenes faecalis, Pseudomonas sp., Pseudomonas fluorescens
-
brenda
Takamura, T.; Ozawa, H.; Soejima, M.
Studies on the induced synthesis of maleate cis-trans isomerase by malonate. Part IV. Catabolite repression and its reversal of maleate cis-trans isomerase
Agric. Biol. Chem.
34
1501-1510
1970
Alcaligenes faecalis, Alcaligenes faecalis IB-14
-
brenda
Takamura, Y.; Takamura, T.; Soejima, M.; Uemura, T.
Studies on the induced synthesis of maleate cis-trans isomerase by malonate. Part III. Purification and properties of maleate cis-trans isomerase induced by malonate
Agric. Biol. Chem.
33
718-728
1969
Alcaligenes faecalis
-
brenda
Scher, W.; Jacoby, W.B.
Maleate isomerase
J. Biol. Chem.
244
1878-1882
1969
Pseudomonas fluorescens
brenda
Takamura, Y.; Nakatani, T.; Soejima, M.; Aoyama, T.
Studies on the induced synthesis of maleate cis-trans isomerase by malonate. Part II. The induction by malonate analogues and the repression by various carbon sources
Agric. Biol. Chem.
32
88-93
1968
Alcaligenes faecalis, Alcaligenes faecalis IB-14
-
brenda
Hatakeyama, K.; Asai, Y.; Uchida, Y.; Kobayashi, M.; Terasawa, M.; Yukawa, H.
Gene cloning and characterization of maleate cis-trans-isomerase from Alcaligenes faecalis
Biochem. Biophys. Res. Commun.
239
74-79
1997
Alcaligenes faecalis
brenda
Hatakeyama, K.; Goto, M.; Kobayashi, M.; Terasawa, M.; Yukawa, H.
Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens
Biosci. Biotechnol. Biochem.
64
1477-1485
2000
Alcaligenes faecalis, Geobacillus stearothermophilus, Serratia marcescens, Serratia marcescens IFO3736
brenda
Fisch, F.; Fleites, C.M.; Delenne, M.; Baudendistel, N.; Hauer, B.; Turkenburg, J.P.; Hart, S.; Bruce, N.C.; Grogan, G.
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 (Q5YXQ1), Nocardia farcinica, Nocardia farcinica IFM 10152 (Q5YXQ1)
brenda
Liu, X.; Zhao, Q.; Ren, J.; Dong, W.; Wu, Q.; Zhu, D.
N-terminal truncation of a maleate cis-trans isomerase from Rhodococcus jostii RHA1 results in a highly active enzyme for the biocatalytic production of fumaric acid
J. Mol. Catal. B
93
44-50
2013
Rhodococcus jostii (Q0SJH2)
-
brenda
Chen, D.; Tang, H.; Lv, Y.; Zhang, Z.; Shen, K.; Lin, K.; Zhao, Y.L.; Wu, G.; Xu, P.
Structural and computational studies of the maleate isomerase from Pseudomonas putida S16 reveal a breathing motion wrapping the substrate inside
Mol. Microbiol.
87
1237-1244
2013
Pseudomonas putida (F8G0M3), Pseudomonas putida S16 (F8G0M3), Pseudomonas putida S16
brenda
Dokainish, H.M.; Ion, B.F.; Gauld, J.W.
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 (Q5YXQ1), Nocardia farcinica IFM 10152 (Q5YXQ1)
brenda
Select items on the left to see more content.
html completed