Information on EC 3.7.1.14 - 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
3.7.1.14
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RECOMMENDED NAME
GeneOntology No.
2-hydroxy-6-oxonona-2,4-dienedioate hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + succinate
show the reaction diagram
(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-phenylpropanoate and 3-(3-hydroxyphenyl)propanoate degradation to 2-oxopent-4-enoate
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cinnamate and 3-hydroxycinnamate degradation to 2-oxopent-4-enoate
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Microbial metabolism in diverse environments
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Phenylalanine metabolism
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3-phenylpropionate degradation
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SYSTEMATIC NAME
IUBMB Comments
(2E,4Z)-2-hydroxy-6-oxona-2,4-dienedioate succinylhydrolase
This enzyme catalyses a step in a pathway of phenylpropanoid compounds degradation. The first step of the enzyme mechanism involves a reversible keto-enol tautomerization [4].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the alpha/beta-hydrolase superfamily
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O
(2E)-2-hydroxypenta-2,4-dienoate + succinate
show the reaction diagram
(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O
(2Z)-2-hydroxypenta-2,4-dienoate + succinate
show the reaction diagram
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the enzyme also catalyses the reverse reaction of C-C hydrolysis, namely C-C bond formation
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r
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid + H2O
?
show the reaction diagram
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MhpC mutant is able to accept the 2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid, on a shorter time scale
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O
(2E)-2-hydroxypenta-2,4-dienoate + succinate
show the reaction diagram
(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O
(2Z)-2-hydroxypenta-2,4-dienoate + succinate
show the reaction diagram
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the enzyme also catalyses the reverse reaction of C-C hydrolysis, namely C-C bond formation
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r
additional information
?
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MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-diketo-nona-1,9-dioic acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.125
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
0.0238
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid
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pH 8.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 12
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
0.036
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid
Escherichia coli
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pH 8.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057 - 4118
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
2386
1.51
2-hydroxy-6-keto-6-phenylhexa-2,4-dienoic acid
Escherichia coli
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pH 8.0, 25°C
41711
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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2 * 31000
31937
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x * 31937, calculated from sequence
62000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 31937, calculated from sequence
homodimer
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2 * 31000
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme structure determination and analysis, PDB ID 1U2E
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hanging drop vapor diffusion method, the X-ray structure of a succinate-H263A MhpC complex shows concerted movements in the positions of both Phe173 and Trp264 that line the approach to Arg188
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hanging-drop vapour-diffusion method. The 2.1 A resolution X-ray structure of the native enzyme determined from orthorhombic crystals confirms that it is a member of the alpha/beta hydrolase fold family, comprising eight beta-strands interconnected by loops and helices. The 2.8 A resolution structure of the enzyme cocrystallized with the non-hydrolysable substrate analogue 2,6-diketo-nona-1,9-dioic acid confirms the location of the active site in a buried channel including Ser110, His263 and Asp235, postulated contributors to a serine protease-like catalytic triad in homologous enzymes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of an engineered 3-(3-hydroxyphenyl)propionate catabolic cassette is analyzed in different gram-negative bacteria
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3-(3-hydroxyphenyl)propionic acid, 3-(2-hydroxyphenyl)propionic acid, 3-(2,3-dihydroxyphenyl)propionic acid or hydrocinnamic acid or cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diol are poor inducers
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C261A
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1.4fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
F173D
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158fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
F173G
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32fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
H263A
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mutant exhibits very slow ketonisation and C-C cleavage
N109A
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125fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
N109H
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217fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
R188K
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217fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
R188Q
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2941fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
S110A
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exhibits fast ketonisation, an intermediate phase, and slow C-C cleavage
S110G
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exhibits fast ketonisation, an intermediate phase, and slow C-C cleavage
S40A
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shows twofold reduced catalytic efficiency, but shows a very fast interconversion of dienol to dienolate forms of the substrate
W264G
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196fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate
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