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Enzyme Nomenclature
Information on EC 5.4.99.14 - 4-Carboxymethyl-4-methylbutenolide mutase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
5.4.99.14
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RECOMMENDED NAME
GeneOntology No.
4-Carboxymethyl-4-methylbutenolide mutase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-Carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide
isomerization does not involve actual methyl migration, but proceeds via the 1-methylbislactone
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide
mechanism
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide
isomerization does not involve actual methyl migration, but proceeds via the 1-methylbislactone
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular transfer reaction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
4-Carboxymethyl-4-methylbut-2-en-1,4-olide methylmutase
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CAS REGISTRY NUMBER
COMMENTARY
115300-03-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
basonym Alcaligenes eutrophus; JMP 134, cloned into Pseudomonas sp. B13 FR1
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme is involved in the modified ortho-cleavage pathway and methylmuconolactone degradation of Ralstonia eutropha strain JMP134
physiological function
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the enzyme is involved in the modified ortho-cleavage pathway and methylmuconolactone degradation of Ralstonia eutropha strain JMP134
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-Carboxymethyl-4-methylbut-2-en-1,4-olide
?
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enzyme of the modified 3-oxoadipate pathway in the Gram-negative bacterium Alcaligenes eutrophus JMP 134
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(4R,5R)-5-chloro-3-methylmuconolactone
trans-3-methyldienelactone
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-
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r
(4R,5R)-5-chloro-3-methylmuconolactone
trans-3-methyldienelactone
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-
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r
(4S,5S)-5-chloro-3-methylmuconolactone
trans-3-methyldienelactone
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-
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r
(4S,5S)-5-chloro-3-methylmuconolactone
trans-3-methyldienelactone
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r
1-Methylbislactone
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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i.e. 1-methyl-3,7-dioxo-2,6-dioxabicyclo[3.3.0]octane
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1-Methylbislactone
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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-
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1-Methylbislactone
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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-
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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-
-
-
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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-
-
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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-
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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-
-
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?
4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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?
4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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highly specific, accepts only (+)-(4S)-4-methylmuconolactone, i.e. 4-carboxymethyl-4-methylbut-2-en-1,4-olide and the putative reaction intermediate 1-methylbislactone
i.e. (-)-(4S)-3-methylmuconolactone
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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highly specific, accepts only (+)-(4S)-4-methylmuconolactone, i.e. 4-carboxymethyl-4-methylbut-2-en-1,4-olide and the putative reaction intermediate 1-methylbislactone
i.e. (-)-(4S)-3-methylmuconolactone
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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4-Carboxymethyl-4-methylbut-2-en-1,4-olide
4-Carboxymethyl-3-methylbut-2-en-1,4-olide
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additional information
?
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not: isomeric methyl-substituted 4-carboxymethylbut-2-en-4-olides
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additional information
?
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activity with 3-methyl-cis,cis-muconate is below the detection limit
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additional information
?
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activity with 3-methyl-cis,cis-muconate is below the detection limit
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-Carboxymethyl-4-methylbut-2-en-1,4-olide
?
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enzyme of the modified 3-oxoadipate pathway in the Gram-negative bacterium Alcaligenes eutrophus JMP 134
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
remaining activity of 6% after incubation with 0.02 mM 4-chloromercuribenzoate for 30 min
additional information
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not: isomeric methyl-substituted 4-carboxymethylbut-2-en-4-olides
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
(4S)-4-methylmuconolactone
mutant enzyme Y39F, in phosphate buffer, 50 mM, pH 7.3
0.052
(4S)-4-methylmuconolactone
wild type enzyme, in phosphate buffer, 50 mM, pH 7.3
0.0972
(4S)-4-methylmuconolactone
mutant enzyme C67S, in phosphate buffer, 50 mM, pH 7.3
0.4583
(4S)-4-methylmuconolactone
mutant enzyme H52A, in phosphate buffer, 50 mM, pH 7.3
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.8
(4S)-4-methylmuconolactone
mutant enzyme Y39F, in phosphate buffer, 50 mM, pH 7.3
7.3
(4S)-4-methylmuconolactone
mutant enzyme C67S, in phosphate buffer, 50 mM, pH 7.3
24.2
(4S)-4-methylmuconolactone
wild type enzyme, in phosphate buffer, 50 mM, pH 7.3
47.2
(4S)-4-methylmuconolactone
mutant enzyme H52A, in phosphate buffer, 50 mM, pH 7.3
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
100
(4S)-4-methylmuconolactone
mutant enzyme C67S, in phosphate buffer, 50 mM, pH 7.3; mutant enzyme H52A, in phosphate buffer, 50 mM, pH 7.3; mutant enzyme Y39F, in phosphate buffer, 50 mM, pH 7.3
500
(4S)-4-methylmuconolactone
wild type enzyme, in phosphate buffer, 50 mM, pH 7.3
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28.8
toward 1-methylbis-lactone, in phosphate buffer, 50 mM, pH 7.3
57.3
toward (4S)-4-methylmuconolactone, in phosphate buffer, 50 mM, pH 7.3
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
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active in this range, rapid decrease of activity above pH 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas reinekei;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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1 * 40000, Alcaligenes eutrophus (JMP 134, cloned into Pseudomonas sp. B13 FR1), SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
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1 * 40000, Alcaligenes eutrophus (JMP 134, cloned into Pseudomonas sp. B13 FR1), SDS-PAGE
tetramer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with (4S)-4-methylmuconolactone and (4S)-3-methylmuconolactone, sitting drop vapor diffusion method, at 19°C, using 25% (w/v) polyethylene glycol 1500, 0.1 M MMT buffer, pH 5 (DL-malic acid, MES, and Tris base in a 1:2:2 molar ratio)
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Chelating agents like EDTA or thiol-group modifying reagents like DTT stabilize
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 24 h, 10% loss of activity, highly purified enzyme, 5% loss of activity with addition of chelating agents like EDTA or thiol-group modifying reagents like DTT
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene mmlI, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C67S
incubation of variant C67S with 4-chloromercuribenzoate does not significantly decrease its activity (above 65% of activity remaining after a 30-min incubation)
H26A
the mutant shows a marked decrease in catalytic activity (kcat) by two orders of magnitude
H52A
the mutation results in an increase in Km by a factor of 9, but only a small change in kcat
Y39F
the mutant displays reduced activity compared to the wild type enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.99.14)
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