2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

This is an abbreviated version!
For detailed information about 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase, go to the full flat file.

Word Map on EC 2.2.1.9

2.2.1.9

menaquinone

thiamin

thdp-dependent

diphosphate-dependent

alpha-ketoglutarate

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic

dioxide

benzoylformate

decarboxylases

stereoselective

hydrolases

alpha/beta

o-succinylbenzoic

metal-ion-dependent

three-domain

two-stage

medium-resolution

Reaction

5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate

Synonyms

(1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, (1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxycyclohex-3-ene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic acid synthase, EC 2.5.1.64, EcMenD, MenD, Rv0555, SEPHCHC synthase, SHCHC synthase

ECTree

2 Transferases

2.2 Transferring aldehyde or ketonic groups

2.2.1 Transketolases and transaldolases

2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

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Results	in table
1	Activating Compound
13334	AA Sequence
1	CAS Registry Number
7	Cloned(Commentary)
10	Cofactor
8	Crystallization (Commentary)
6	General Information
3	General Stability
3	IC50 Value
5	Inhibitors
37	kcat/KM [mM/s]
3	Ki Value [mM]
44	KM Value [mM]
7	Metals/Ions
3	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
207	Organism
6	Pathway
153	PDB ID
3	pH Optimum
34	Protein Variants
8	Purification (Commentary)
4	Reaction
1	Reaction Type
17	Reference
1	Storage Stability
43	Substrates and Products (Substrate)
7	Subunits
41	Synonyms
1	Systematic Name
1	Temperature Stability [°C]
41	Turnover Number [1/s]

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General Information on EC 2.2.1.9 - 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

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evolution

Escherichia coli

P17109

the enzyme Men D is not significantly different from other ThDP-dependent enzymes in active-site architecture, cofactor binding, or overall three-dimensional structure, suggesting the use of the canonical enamine intermediate in its catalysis

745170

metabolism

2 entries

physiological function

2 entries

additional information

Escherichia coli

P17109

in the covalent tetrahedral enamine intermediate, all of the bond lengths and angles of its planar thiazolium ring are comparable to those of a similar enzyme-free thiamine diphosphate adduct, complex crystal structure determination and analysis, NMR structure analysis and modeling, overview

745170