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Literature summary for 3.7.1.14 extracted from

  • Li, C.; Li, J.J.; Montgomery, M.G.; Wood, S.P.; Bugg, T.D.
    Catalytic role for arginine 188 in the C-C hydrolase catalytic mechanism for Escherichia coli MhpC and Burkholderia xenovorans LB400 BphD (2006), Biochemistry, 45, 12470-12479.
    View publication on PubMed
Search for more literature for 3.7.1.14

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Escherichia coli

Protein Variants

Protein Variants Comment Organism
C261A 1.4fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli
F173D 158fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli
F173G 32fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli
N109A 125fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli
N109H 217fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli
R188K 217fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli
R188Q 2941fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli
W264G 196fold decrease in kcat/Km for (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.004
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme N109A Escherichia coli
0.004
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme N109H Escherichia coli
0.0042
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme C261A Escherichia coli
0.0068
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°, wild-type enzyme Escherichia coli
0.01
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme F173D Escherichia coli
0.038
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme R188K Escherichia coli
0.058
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme F173G Escherichia coli
0.077
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme R188Q Escherichia coli
0.125
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme W264G 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

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-ketonona-2,4-diene-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
0.08
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme N109H Escherichia coli
0.1
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme R188Q Escherichia coli
0.13
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme N109A Escherichia coli
0.26
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme F173D Escherichia coli
0.74
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme R188K Escherichia coli
2 8 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°, wild-type enzyme Escherichia coli
2.7
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme W264G Escherichia coli
7.5
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme F173G Escherichia coli
12
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme C261A 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
1.4
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme R188Q Escherichia coli
19
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme N109H Escherichia coli
19
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme R188K Escherichia coli
21
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme W264G Escherichia coli
26
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme F173D Escherichia coli
33
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme N109A Escherichia coli
130
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme F173G Escherichia coli
2900
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°C, mutant enzyme C261A Escherichia coli
4118
-
 (2E,4Z)-2-hydroxy-6-oxonona-2,4-dienedioate pH 8.0, 25°, wild-type enzyme Escherichia coli