Literature summary for 3.7.1.14 extracted from

Dunn, G.; Montgomery, M.G.; Mohammed, F., Coker, A.; Cooper, J.B.; Robertson, T.; Garcia, J.L.; Bugg, T.D.; Wood, S.P.
The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism (2005), J. Mol. Biol., 346, 253-265.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Escherichia coli

Crystallization (Comment)

Organism

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

Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
2,6-diketo-nona-1,9-dioic acid	-	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
31000	-	2 * 31000	Escherichia coli
62000	-	gel filtration	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	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(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	-	?

Subunits

Subunits	Comment	Organism
homodimer	2 * 31000	Escherichia coli

Synonyms

Synonyms	Comment	Organism
2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase	-	Escherichia coli
MhpC	-	Escherichia coli

General Information

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