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Literature summary for 3.7.1.14 extracted from

  • Li, C.; Montgomery, M.G.; Mohammed, F.; Li, J.J.; Wood, S.P.; Bugg, T.D.
    Catalytic mechanism of C-C hydrolase MhpC from Escherichia coli: kinetic analysis of His263 and Ser110 site-directed mutants (2005), J. Mol. Biol., 346, 241-251.
    View publication on PubMed
Search for more literature for 3.7.1.14

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
H114A shows twofold-reduced catalytic efficiency, ruling out a catalytic role, but shows a fivefold-reduced KM for the natural substrate, and an ability to process an aryl-containing substrate, implying a role for His114 in positioning of the substrate Escherichia coli
H263A mutant exhibits very slow ketonisation and C-C cleavage Escherichia coli
S110A exhibits fast ketonisation, an intermediate phase, and slow C-C cleavage Escherichia coli
S110G exhibits fast ketonisation, an intermediate phase, and slow C-C cleavage Escherichia coli
S40A shows twofold reduced catalytic efficiency, but shows a very fast interconversion of dienol to dienolate forms of the substrate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S40A Escherichia coli
0.0025
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme H114A Escherichia coli
0.0055
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme H263A Escherichia coli
0.0068
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, wild-type enzyme Escherichia coli
0.0175
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S110G Escherichia coli
0.0185
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S110A Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O Escherichia coli the enzyme is involved in 3-phenylpropanoate catabolism (2E)-2-hydroxypenta-2,4-dienoate + succinate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P77044
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + succinate a catalytic mechanism is proposed involving stabilisation of reactive intermediates and activation of a nucleophilic water molecule by Ser110 Escherichia coli
a
(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate a catalytic mechanism is proposed involving stabilisation of reactive intermediates and activation of a nucleophilic water molecule by Ser110 Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O
-
 Escherichia coli (2E)-2-hydroxypenta-2,4-dienoate + succinate
-
 ?
(2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O the enzyme is involved in 3-phenylpropanoate catabolism Escherichia coli (2E)-2-hydroxypenta-2,4-dienoate + succinate
-
 ?

Synonyms

Synonyms Comment Organism
2-hydroxy-6-keto-nona-1,9-dioic acid 5,6-hydrolase
-
 Escherichia coli
MhpC
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.001
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S110G Escherichia coli
0.0029
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme H263A Escherichia coli
0.0054
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S110A Escherichia coli
0.016
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme D235A, approximate value from activity of the cell extract Escherichia coli
2 8 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, wild-type enzyme Escherichia coli
2.9
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S40A Escherichia coli
4.5
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme H114A Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme is involved in 3-phenylpropanoate catabolism Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.057
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S110G Escherichia coli
0.29
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S110A Escherichia coli
5.27
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme H263A Escherichia coli
242
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme S40A Escherichia coli
412
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, wild-type enzyme Escherichia coli
1800
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme H114A Escherichia coli