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Information on EC 4.1.2.61 - feruloyl-CoA hydratase/lyase
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4.1.2.61 feruloyl-CoA hydratase/lyaseIUBMB Comments
The enzyme is a member of the enoyl-CoA hydratase/isomerase superfamily. It catalyses a two-step process involving first the hydration of the double bond of feruloyl-CoA and then the cleavage of the resultant beta-hydroxy thioester by retro-aldol reaction. (E)-caffeoyl-CoA and (E)-4-coumaroyl-CoA are also substrates.
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Word Map
- 4.1.2.61
-
ferulic
-
phenylpropanoid
- vanilla
- 4-hydroxybenzaldehyde
- lignin
-
caffeic
-
hydroxycinnamoyl-coas
- amycolatopsis
- p-coumaroyl-coa
- planifolia
-
4-coumaric
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
enoyl-coa hydratase/aldolase, vanillin synthase, 4-hydroxycinnamoyl-coa hydratase/lyase, hydroxycinnamoyl-coa hydratase/lyase, feruloyl-coa hydratase/lyase, feruloyl-coa hydratase-lyase, 4-hydroxycinnamoyl-coenzyme a hydratase-lyase, pphchl, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy-3-(4-hydroxyl-3-methoxyphenyl)propanoyl-CoA vanillin lyase (acetyl-CoA-forming)
-
-
4-hydroxycinnamoyl-CoA hydratase/lyase
4-hydroxycinnamoyl-coenzyme A hydratase-lyase
couA
-
-
-
-
EC 4.1.2.41
-
-
formerly
-
EC 4.2.1.101
-
-
formerly
-
enoyl-CoA hydratase/aldolase
FCHL
FerB
-
-
ambiguous
-
feruloyl-CoA hydratase-lyase
HCHL
hydroxycinnamoyl-CoA hydratase lyase
-
-
-
-
hydroxycinnamoyl-CoA hydratase/lyase
PpHCHL
VAN
vanillin synthase
-
-
-
-
4-hydroxycinnamoyl-CoA hydratase/lyase
-
enzyme has hydratase and lyase activity
4-hydroxycinnamoyl-CoA hydratase/lyase
-
enzyme has hydratase and lyase activity
-
enoyl-CoA hydratase/aldolase
-
-
ambiguous
-
HCHL
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA = feruloyl-CoA + H2O
-
-
-
-
feruloyl-CoA + H2O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
(1a)
-
-
-
feruloyl-CoA + H2O = vanillin + acetyl-CoA
overall reaction
-
-
-
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA = vanillin + acetyl-CoA
involved, together with EC 4.2.1.101 trans-feruloyl-CoA hydratase, in the production of vanillin from trans-ferulic acid. Vanillin is converted to vanillate by EC 1.2.1.67 vanillin dehydrogenase
-
-
-
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA = vanillin + acetyl-CoA
(1b)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cleavage of a C-O bond
-
-
-
-
reversal of an aldol condensation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
feruloyl-CoA hydro-lyase/vanillin-lyase (acetyl-CoA-forming)
The enzyme is a member of the enoyl-CoA hydratase/isomerase superfamily. It catalyses a two-step process involving first the hydration of the double bond of feruloyl-CoA and then the cleavage of the resultant beta-hydroxy thioester by retro-aldol reaction. (E)-caffeoyl-CoA and (E)-4-coumaroyl-CoA are also substrates.
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CAS REGISTRY NUMBER
COMMENTARY
197462-62-7
-
197462-63-8
-
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SUBSTRATE
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-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
4-feruloyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
i.e. vanillin
ir
4-hydroxy-3-methoxy-phenyl-beta-hydroxypropionyl-CoA + H2O
vanillin + acetylCoA + feruloylCoA
-
-
-
?
4-hydroxy-3-methoxycinnamoyl-CoA + H2O
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
feruloyl-CoA + H2O
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
p-coumaroyl-CoA
4-hydroxy-3-methoxy-benzaldehyde + acetyl-CoA
-
in transgenic plants the HCHL enzyme acts upon intermediates of the phenylpropanoid pathway
i.e. vanillin
-
?
3,4-dihydroxycinnamoyl-CoA + H2O
3,4-dihydroxybenzaldehyde + acetyl-CoA
-
-
-
?
3,4-dihydroxycinnamoyl-CoA + H2O
3,4-dihydroxybenzaldehyde + acetyl-CoA
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
vanillin + acetyl-CoA
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
Streptomyces viridosporus T7A / ATCC 39115
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
Streptomyces viridosporus T7A / ATCC 39115
-
-
-
-
?
4-coumaroyl-CoA
4-hydroxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxycinnamoyl-CoA
-
?, ir
4-coumaroyl-CoA
4-hydroxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxycinnamoyl-CoA
-
?, ir
4-coumaroyl-CoA + H2O
4-hydroxybenzaldehyde + acetyl-CoA
-
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxycinnamoyl-CoA + H2O
4-hydroxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxycinnamoyl-CoA + H2O
4-hydroxybenzaldehyde + acetyl-CoA
-
-
-
?
4-trans-feruloyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
i.e. vanillin
?
4-trans-feruloyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
i.e. vanillin
?
caffeoyl-CoA
3,4-dihydroxybenzaldehyde + acetyl-CoA
-
i.e. 3,4-dihydroxycinnamoyl-CoA
i.e. protocatechuic aldehyde
?, ir
caffeoyl-CoA
3,4-dihydroxybenzaldehyde + acetyl-CoA
-
i.e. 3,4-dihydroxycinnamoyl-CoA
i.e. protocatechuic aldehyde
?, ir
feruloyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
modelling of the natural substrate feruloyl-CoA in the active site of HCHL reveals a catalytic role for Glu143 and a substrate-specific evidence for Tyr239 from the adjacent monomeric structure
catalyzes the hydration of the acyl-CoA thioester of ferulic acid, hydration of the double bond yields 4-hydroxy-3-methoxy-phenyl-beta-hydroxy-propionyl-CoA, subsequent retro-aldol cleavage leads to vanilin
-
?
feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
first step of reaction
-
-
?
feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
first step of reaction
-
-
?
feruloyl-CoA + H2O
vanillin + acetyl-CoA
overall reaction
-
-
?
feruloyl-CoA + H2O
vanillin + acetyl-CoA
overall reaction
-
-
?
feruloyl-CoA + H2O
vanillin + acetyl-CoA
the enzyme is required for p-coumarate degradation
-
-
?
feruloyl-CoA + H2O
vanillin + acetyl-CoA
-
-
-
?
feruloyl-CoA + H2O
vanillin + acetyl-CoA
the enzyme is required for p-coumarate degradation
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
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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-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
4-feruloyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
i.e. vanillin
ir
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
feruloyl-CoA + H2O
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
-
-
-
-
?
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propionyl-CoA
vanillin + acetyl-CoA
Streptomyces viridosporus T7A / ATCC 39115
-
-
-
-
?
4-coumaroyl-CoA
4-hydroxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxycinnamoyl-CoA
-
ir
4-coumaroyl-CoA
4-hydroxybenzaldehyde + acetyl-CoA
-
i.e. 4-hydroxycinnamoyl-CoA
-
ir
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
4-hydroxy-3-methoxybenzaldehyde + acetyl-CoA
-
-
-
?
caffeoyl-CoA
3,4-dihydroxybenzaldehyde + acetyl-CoA
-
i.e. 3,4-dihydroxycinnamoyl-CoA
i.e. protocatechuic aldehyde
ir
caffeoyl-CoA
3,4-dihydroxybenzaldehyde + acetyl-CoA
-
i.e. 3,4-dihydroxycinnamoyl-CoA
i.e. protocatechuic aldehyde
ir
feruloyl-CoA + H2O
vanillin + acetyl-CoA
the enzyme is required for p-coumarate degradation
-
-
?
feruloyl-CoA + H2O
vanillin + acetyl-CoA
the enzyme is required for p-coumarate degradation
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
trans-feruloyl-CoA + H2O
4-hydroxy-3-methoxyphenyl-beta-hydroxypropionyl-CoA
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
no activity for mutant enzymes E143A and S123A/E143A
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
no activity for mutant enzymes E143A and S123A/E143A
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activity measured, quantification by integration of peaks with reference to vanillin, peak identity calculated by GC-MS and NMR
additional information
-
enzyme activity in several transgenic cell lines from hairy roots of Datura stramonium
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 9.5
-
in Tris-HCl or borate buffer, activity declined to ca. 50% of its maximum at pH 6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
transgenic tobacco cv XHFD 8 expressing various levels of HCHL, the bacterial 4-hydroxycinnamoyl-CoA hydratase/lyase gene of Pseudomonas fluorescens, transgenic lines 201 and 27 reveal high expression, line 13 shows intermediate expression, pBin 19 plants serve as controls
-
-
brenda
feruloyl-CoA hydratase-lyase from a lignin-degrading consortium
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
young leaves from pre- and postflowering transgenic and control plants, cell wall components analysed by HPLC, plants expressing high levels of HCHL exhibit a reduced lignin deposition, monolignol biosynthesis and vascular integrity impaired
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
impact on cell wall integrity and vascular integrity, biomechanical tissue properties, carbon allocation to phenolic pools, lignin formation studied, morphological changes of the plants described
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the ferB mutant FBK is scarcely able to transform feruloyl-CoA
metabolism
physiological function
metabolism
the enzyme catalyzes a step in the catabolic pathway of ferulate
metabolism
the enzyme is involved in the vanillin production from ferulic acid
physiological function
the enzyme is required for p-coumarate degradation
physiological function
-
the enzyme is required for p-coumarate degradation
-
Show AA Sequence and Transmembrane Helices (742 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
198000
dynamic light scattering and circular dichroism spectroscopy
31000
31007
-
6 * 31007, crystallization, calculated from amino acid sequence
31000
-
alpha, alpha, 2 * 31000, SDS-PAGE, deduced from gene sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
additional information
-
hexameric structure of two stacked trimers assumed, similarities to the crotonase superfamily
dimer
-
alpha, alpha, 2 * 31000, SDS-PAGE, deduced from gene sequence
dimer
-
alpha, alpha, 2 * 31000, SDS-PAGE, deduced from gene sequence
-
hexamer
-
6 * 31007, crystallization, calculated from amino acid sequence
hexamer
-
6 * 31007, crystallization, calculated from amino acid sequence
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.8 A resolution, data collection and refinement statistics shown, structure solution and in silico modelling determined, monomer folding and factors affecting trimer assembly indicated, oligo structure and modelling of the active site determined
-
by the hanging-drop method of vapour diffusion using polyethylene glycol 20000 Da as the precipitant, 1.8 A resolution
-
hanging-drop vapour diffusion method, wild-type hydroxycinnamoyl-CoA hydratase/lyase in complex with acetyl-CoA and vanillin 2vss: protein concentration of 10 mg/ml in 11% (w/v) PEG [poly(ethylene glycol)] (20000 Da) with 8% PEG (550 Da) monomethyl ether, 0.8 M sodium formate and 0.2% (v/v) butane 1,4-diol in 0.05 M Mes buffer (pH 5.6), 10 mM feruloyl.CoA, resolution 2.22 A, space group P 21 21 21. A ternary complex of hydroxycinnamoyl-CoA hydratase/lyase mutant S123A (HCHL) with acetyl-CoA and vanillin gives insights into substrate specificity and mechanism 2vsu: resolution 1.9 A, space group P 21 21 21
sitting drop vapor diffusion method, crystal structure is solved and refined at 2.1 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S123A
mutation of Ser123 to alanine results in a mutant displaying a reduced turnover nummber compared with the wild-type and a KM comparable with that of the wild-type, suggesting that there is little contribution of this residue to mechanism or substrate binding
Y239F
Tyr239 is an important residue in determining substrate specificity
S123A
-
mutation of Ser123 to alanine results in a mutant displaying a reduced turnover nummber compared with the wild-type and a KM comparable with that of the wild-type, suggesting that there is little contribution of this residue to mechanism or substrate binding
-
Y239F
-
Tyr239 is an important residue in determining substrate specificity
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
the enzyme is very stable and remains undissociated even under extreme pH conditions
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very stable and remains undissociated even under extreme pH conditions
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-affinity chromatography, the histidine tags are removed
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21 to yield HCHL protein encoded by Pseudomonas fluorescens strain AN103
-
expressed in Escherichia coli Survival 2 T1 cells and in Capsicum frutescens cultivar Hot Lava
-
functional expression in hairy root cells of Datura stramonium via infection with Agrobacterium rhizogenes, no accumulation of 4-hydroxybenzaldehyde derivatives occurs, but diminished feruloyl-CoA availability, leading to reduced lignin formation, and formation of new glucoconjugates of 4-hydroxybenzaldehyde derivatives, e.g. 4-hydroxybenzyl alcohol-O-beta-D-glucoside
-
gene encoding an enoyl-SCoA hydratase/lyase isolated, cloned and heterologously expressed in Escherichia coli JM109
-
gene ferB, the ferBA genes form an operon, genetic organization of the fer gene cluster, overview. Transcriptional regulation of ferBA controlled by a MarR-type transcriptional regulator, FerC. The ferC gene is located upstream of ferB. The transcription start site of ferB is mapped at 30 nucleotides upstream from the ferB initiation codon. Constitutive expression of the ferC-ferB intergenic region in SME043 cells, FerC regulates the ferBA transcription through the binding to the ferCferB intergenic region
Phyllostachys nigra cells are transformed to express 4-hydroxycinnamoyl-CoA hydratase/lyase. The PpHCHL-transformed cells accumulate glucose conjugates of 4-hydroxybenzoic acid and vanillic acid, indicating that the PpHCHL products (aldehydes) are further metabolized by inherent enzymes in the Phyllostachys nigra cells
-
transgenic tobacco cv. XHFD 8 plants expressing various levels of bacterial HCHL, lignin deposition reduced, monolignol biosynthesis and vascular integrity impaired, reduction in stem toughness, cell wall esterified and soluble phenolics reduced, wall-bound accretion of vanillin and vanillic acid, intracellular accumulation of novel metabolites such as hydroxybenzoic and vanillic acid derivatives
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression increases with flavour development from first stage to second stage
-
Rpa1794 (CouR) represses couAB expression
there is a decrease in enzyme expression from 19.2fold to 5.2fold for second stage to third stage of flavour development
-
transcription of ferB is induced 6.5fold in the SYK-6 cells grown on ferulate
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
additional information
synthesis
-
useful for commercial microbial batch fermentation of vanillin, economical production of vanillic acid instead of chemical oxidation of vanillin
synthesis
Streptomyces viridosporus T7A / ATCC 39115
-
useful for commercial microbial batch fermentation of vanillin, economical production of vanillic acid instead of chemical oxidation of vanillin
-
additional information
-
modelling data as a prerequisite for enzyme engineering
additional information
-
studies on genetic manipulation of cell walls in plants
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Narbad, A.; Gasson, M.J.
Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly isolated strain of Pseudomonas fluorescens
Microbiology
144
1397-1405
1998
Bacillus subtilis, Corynebacterium glutamicum, Burkholderia cepacia, Delftia acidovorans, Escherichia coli, Pseudomonas fluorescens, Streptomyces griseus
brenda
Pometto, A.L.; Crawford, D.L.
Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus
Appl. Environ. Microbiol.
45
1582-1585
1983
Streptomyces viridosporus, Streptomyces viridosporus T7A / ATCC 39115
brenda
Mitra, A.; Kitamura, Y.; Gasson, M.J.; Narbad, A.; Parr, A.J.; Pyne, J.; Rhodes, M.J.C.; Sewter, C.; Walton, N.J.
4-Hydroxycinnamoyl-CoA hydratase/lyase (HCHL)-an enzyme of phenylpropanoid chain cleavage from Pseudomonas
Arch. Biochem. Biophys.
365
10-16
1999
Pseudomonas fluorescens, Pseudomonas fluorescens AN103
brenda
Overhage, J.; Priefert, H.; Steinbuchel, A.
Biochemical and genetic analysis of ferulic acid catabolism in Pseudomonas sp. strain HR199
Appl. Environ. Microbiol.
65
4837-4847
1999
Pseudomonas sp., Pseudomonas sp. HR 199
brenda
Gasson, M.J.; Kitamura, Y.; McLauchlan, W.R.; Narbad, A.; Parr, A.J.; Parsons, E.L.; Payne, J.; Rhodes, M.J.; Walton, N.J.
Metabolism of ferulic acid to vanillin. A bacterial gene of the enoyl-SCoA hydratase/isomerase superfamily encodes an enzyme for the hydration and cleavage of a hydroxycinnamic acid SCoA thioester
J. Biol. Chem.
273
4163-4170
1998
Delftia acidovorans, Pseudomonas fluorescens
brenda
Mitra, A.; Mayer, M.J.; Mellon, F.A.; Michael, A.J.; Narbad, A.; Parr, A.J.; Waldron, K.W.; Walton, N.J.
4-Hydroxycinnamoyl-CoA hydratase/lyase, an enzyme of phenylpropanoid cleavage from Pseudomonas, causes formation of C(6)-C(1) acid and alcohol glucose conjugates when expressed in hairy roots of Datura stramonium L.
Planta
215
79-89
2002
Pseudomonas fluorescens, Pseudomonas fluorescens AN103
brenda
Leonard, P.M.; Marshall, C.M.; Dodson, E.J.; Walton, N.J.; Grogan, G.
Purification, crystallization and preliminary x-ray crystallographic analysis of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL), a crotonase homologue active in phenylpropanoid metabolism
Acta Crystallogr. Sect. D
D60
2343-2345
2004
Pseudomonas fluorescens, Pseudomonas fluorescens AN103
brenda
Leonard, P.M.; Brzozowski, A.M.; Lebedev, A.; Marshall, C.M.; Smith, D.J.; Verma, C.S.; Walton, N.J.; Grogan, G.
The 1.8 A resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin
Acta Crystallogr. Sect. D
62
1494-1501
2006
Pseudomonas fluorescens
brenda
Merali, Z.; Mayer, M.J.; Parker, M.L.; Michael, A.J.; Smith, A.C.; Waldron, K.W.
Metabolic diversion of the phenylpropanoid pathway causes cell wall and morphological changes in transgenic tobacco stems
Planta
225
1165-1178
2007
Nicotiana tabacum
brenda
Bennett, J.P.; Bertin, L.; Moulton, B.; Fairlamb, I.J.; Brzozowski, A.M.; Walton, N.J.; Grogan, G.
A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) with acetyl-CoA and vanillin gives insights into substrate specificity and mechanism
Biochem. J.
414
281-289
2008
Pseudomonas fluorescens (O69762), Pseudomonas fluorescens AN103 (O69762)
brenda
Botosoa, E.P.; Blumenstein, C.; MacKenzie, D.A.; Silvestre, V.; Remaud, G.S.; Kwiecien, R.A.; Robins, R.J.
Quantitative isotopic 13C nuclear magnetic resonance at natural abundance to probe enzyme reaction mechanisms via site-specific isotope fractionation: the case of the chain-shortening reaction for the bioconversion of ferulic acid to vanillin
Anal. Biochem.
393
182-188
2009
Streptomyces griseus
brenda
Kasai, D.; Kamimura, N.; Tani, K.; Umeda, S.; Abe, T.; Fukuda, M.; Masai, E.
Characterization of FerC, a MarR-type transcriptional regulator, involved in transcriptional regulation of the ferulate catabolic operon in Sphingobium sp. strain SYK-6
FEMS Microbiol. Lett.
332
68-75
2012
Sphingobium sp. (G2IJ08), Sphingobium sp.
brenda
Kiran, K.; Sonbarse, P.P.; Veeresh, L.; Shetty, N.P.; Parvatam, G.
Expression profile of phenylpropanoid pathway genes in Decalepis hamiltonii tuberous roots during flavour development
3 Biotech
8
365
2018
Decalepis hamiltonii
brenda
Chee, M.J.; Lycett, G.W.; Khoo, T.J.; Chin, C.F.
Bioengineering of the plant culture of Capsicum frutescens with vanillin synthase gene for the production of vanillin
Mol. Biotechnol.
59
1-8
2017
Vanilla planifolia
brenda
Yang, H.; Barros-Rios, J.; Kourteva, G.; Rao, X.; Chen, F.; Shen, H.; Liu, C.; Podstolski, A.; Belanger, F.; Havkin-Frenkel, D.; Dixon, R.A.
A re-evaluation of the final step of vanillin biosynthesis in the orchid Vanilla planifolia
Phytochemistry
139
33-46
2017
no activity in Vanilla planifolia
brenda
Hirakawa, H.; Schaefer, A.L.; Greenberg, E.P.; Harwood, C.S.
Anaerobic p-coumarate degradation by Rhodopseudomonas palustris and identification of CouR, a MarR repressor protein that binds p-coumaroyl coenzyme A
J. Bacteriol.
194
1960-1967
2012
Rhodopseudomonas palustris (Q6N8W7), Rhodopseudomonas palustris ATCC BAA-98 (Q6N8W7)
brenda
Yang, W.; Tang, H.; Ni, J.; Wu, Q.; Hua, D.; Tao, F.; Xu, P.
Characterization of two Streptomyces enzymes that convert ferulic acid to vanillin
PLoS One
8
e67339
2013
Streptomyces sp. (S5LPF1), Streptomyces sp.
brenda
Liberato, M.V.; Araujo, J.N.; Sodre, V.; Goncalves, T.A.; Vilela, N.; Moraes, E.C.; Garcia, W.; Squina, F.M.
The structure of a prokaryotic feruloyl-CoA hydratase-lyase from a lignin-degrading consortium with high oligomerization stability under extreme pHs
Biochim. Biophys. Acta
1868
140344
2020
uncultured organism (A0A2P1BT02)
brenda
Kitaoka, N.; Nomura, T.; Ogita, S.; Kato, Y.
Bioproduction of glucose conjugates of 4-hydroxybenzoic and vanillic acids using bamboo cells transformed to express bacterial 4-hydroxycinnamoyl-CoA hydratase/lyase
J. Biosci. Bioeng.
S1389-1723
30926-0
2020
Pseudomonas putida, Pseudomonas putida KT 2440
brenda
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