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
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4.1.1.7
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thiamin
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putida
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thdp-dependent
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diphosphate-dependent
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carboligation
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carboligase
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acyloin
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r-benzoin
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synthesis
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s-mandelate
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2-keto
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biotechnology
- 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
4.1.1.7 benzoylformate decarboxylaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 4.1.1.7 - benzoylformate decarboxylase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-ethoxy-4-hydroxybenzoylformate
ethyl vanillin + CO2
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?
Benzoylformate
?
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enzyme is involved in the inducible pathway of mandelate
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?
Benzoylformate
?
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enzyme is involved in the metabolism of mandelic acid
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?
Benzoylformate
?
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enzyme is involved in the metabolism of mandelic acid
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?
Benzoylformate
?
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enzyme is involved in the inducible pathway of mandelate
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?
Benzoylformate
?
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enzyme is involved in the metabolism of mandelic acid
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?
Benzoylformate
?
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enzyme is involved in the metabolic pathway of phenylglycine
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?
Benzoylformate
?
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enzyme is involved in the metabolic pathway of phenylglycine
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?
Benzoylformate
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the enzyme is involved in the pathway for catabolism of D(+)-mandelate and L-(-)-mandelate
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?
additional information
?
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the enzyme performs enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes
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?
additional information
?
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when 3-ethoxy-4-hydroxybenzoylformate is provided at with Pseudomonas putida, it is completely transformed to ethyl vanillic acid after 2 days, but only trace amounts of ethyl vanillin are detected. Similar results are obtained when ethyl vanillin replaces 3-ethoxy-4-hydroxybenzoylformate as substrate, thus aldehyde dehydrogenation activity in Pseudomonas putida is greater than its synthesis activity. The recombinant Escherichia coli strain expressing the enzyme from Pseudomonas putida converts (S)-3-ethoxy-4-hydroxymandelic acid into ethyl vanillin, but does not degrade ethyl vanillin, overview
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?
additional information
?
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when 3-ethoxy-4-hydroxybenzoylformate is provided at with Pseudomonas putida, it is completely transformed to ethyl vanillic acid after 2 days, but only trace amounts of ethyl vanillin are detected. Similar results are obtained when ethyl vanillin replaces 3-ethoxy-4-hydroxybenzoylformate as substrate, thus aldehyde dehydrogenation activity in Pseudomonas putida is greater than its synthesis activity. The recombinant Escherichia coli strain expressing the enzyme from Pseudomonas putida converts (S)-3-ethoxy-4-hydroxymandelic acid into ethyl vanillin, but does not degrade ethyl vanillin, overview
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?
additional information
?
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when 3-ethoxy-4-hydroxybenzoylformate is provided at with Pseudomonas putida, it is completely transformed to ethyl vanillic acid after 2 days, but only trace amounts of ethyl vanillin are detected. Similar results are obtained when ethyl vanillin replaces 3-ethoxy-4-hydroxybenzoylformate as substrate, thus aldehyde dehydrogenation activity in Pseudomonas putida is greater than its synthesis activity. The recombinant Escherichia coli strain expressing the enzyme from Pseudomonas putida converts (S)-3-ethoxy-4-hydroxymandelic acid into ethyl vanillin, but does not degrade ethyl vanillin, overview
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?
