4.1.1.7: benzoylformate decarboxylase

This is an abbreviated version!
For detailed information about benzoylformate decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.7

4.1.1.7

thiamin

putida

thdp-dependent

diphosphate-dependent

carboligation

carboligase

acyloin

r-benzoin

synthesis

s-mandelate

2-keto

biotechnology

Reaction

Synonyms

benzoylformate decarboxylase, BFD, BfdB, BFDC, BfdM, Decarboxylase, benzoylformate, MdlC, Phenylglyoxylate decarboxylase

ECTree

4 Lyases

4.1 Carbon-carbon lyases

4.1.1 Carboxy-lyases

4.1.1.7 benzoylformate decarboxylase

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Results	in table
1	Activating Compound
1360	AA Sequence
6	Application
1	CAS Registry Number
23	Cloned(Commentary)
36	Cofactor
10	Crystallization (Commentary)
4	General Information
7	General Stability
32	Inhibitors
52	kcat/KM [mM/s]
14	Ki Value [mM]
134	KM Value [mM]
17	Metals/Ions
8	Molecular Weight [Da]
22	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
112	Organism
10	Pathway
96	PDB ID
13	pH Optimum
2	pH Range
6	pH Stability
96	Protein Variants
26	Purification (Commentary)
2	Reaction
7	Reaction Type
66	Reference
16	Source Tissue
7	Specific Activity [micromol/min/mg]
8	Storage Stability
250	Substrates and Products (Substrate)
13	Subunits
47	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
1	Temperature Range [°C]
87	Turnover Number [1/s]

General Information

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General Information on EC 4.1.1.7 - benzoylformate decarboxylase

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metabolism

Pseudomonas putida

penultimate enzyme in the mandelate pathway, that catalyzes the non-oxidative decarboxylation of benzoylformate to yield carbon dioxide and benzaldehyde

727483

physiological function

2 entries

additional information

Pseudomonas putida

the first step in catalysis by all ThDP-dependent enzymes is the deprotonation of the C2 carbon by the 4'-imino group to form the ylide. Both active sites contain two histidine residues in the catalytic dimer, three ionizable residues in the active site of the enzyme are Ser26, His70 and His281. His281 is the donor for the protonation of the enamine intermediate, Ser26 forms a hydrogen bond with the carboxylate of the substrate

727483