Information on EC 2.3.1.246 - 3,5-dihydroxyphenylacetyl-CoA synthase

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The expected taxonomic range for this enzyme is: Amycolatopsis

EC NUMBER
COMMENTARY hide
2.3.1.246
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RECOMMENDED NAME
GeneOntology No.
3,5-dihydroxyphenylacetyl-CoA synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 malonyl-CoA = (3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of vancomycin group antibiotics
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:malonyl-CoA malonyltransferase (3,5-dihydroxyphenylacetyl-CoA-forming)
The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the nonproteinogenic amino acid (S)-3,5-dihydroxyphenylglycine, a component of the vancomycin-type antibiotic balhimycin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
inactivation of dpgA results in loss of balhimycin production, and restoration is achieved by supplementation with 3,5-dihydroxyphenylacetate
physiological function
the enzyme is involved in the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine, a component of the vancomycin-type antibiotic balhimycin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4 malonyl-CoA
(3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
show the reaction diagram
4 malonyl-CoA
3,5-dihydroxyphenylacetyl-CoA + 3 CoA + 4 CO2 + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4 malonyl-CoA
(3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
show the reaction diagram
Q939X3
the enzyme is involved in the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine, a component of the vancomycin-type antibiotic balhimycin
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?
4 malonyl-CoA
3,5-dihydroxyphenylacetyl-CoA + 3 CoA + 4 CO2 + H2O
show the reaction diagram
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the enzyme is involved in biosynthesis of 3,5-dihydroxyphenylglycine, a key nonproteinogenic residue in the vancomycin family of antibiotics
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.13
malonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029 - 0.0135
malonyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.9
malonyl-CoA
76
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41593
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2 * 41593, electrospray mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 41593, electrospray mass spectrometry
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Streptomyces lividans
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C160A
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kcat/Km for malonyl-CoA is 0.16% compared to the kcat/Km-value of the wild-type enzyme. The mutant shows an increased partition ratio for malonyl-CoA decarboxylation to acetyl-CoA vs condensation to 3,5-dihydroxyphenylacetyl-CoA, reflecting more uncoupling in the mutant enzyme
C160S
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kcat/Km for malonyl-CoA is 2.3% compared to the kcat/Km-value of the wild-type enzyme
C190A
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mutant retains wild-type activity
H296A
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mutant has a 6fold drop in kcat
C160A/C190A
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formation of (3,5-dihydroxyphenylacetyl)-CoA is barely detectable