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Information on EC 2.3.1.246 - 3,5-dihydroxyphenylacetyl-CoA synthase
for references in articles please use BRENDA:EC2.3.1.246
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.246 3,5-dihydroxyphenylacetyl-CoA synthase
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
showSynonyms
dpgA, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dpgA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 malonyl-CoA = (3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 malonyl-CoA
(3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
Substrates: 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
Products: -
Products: -
?
4 malonyl-CoA
(3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
Substrates: -
Products: -
Products: -
?
4 malonyl-CoA
(3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
-
Substrates: diketyl-CoA and triketyl-CoA are confirmed to be the intermediates in the enzyme catalyzed synthesis of (3,5-dihydroxyphenylacetyl)-CoA. Polyketone intermediates alternate between the Cys160 residue and CoA through transthioesterification reactions, in which the chain is elongated by enolate attack on the thioester carbon of the enzyme-bound (poly)ketide intermediate by decarboxylation in malonyl-CoA or polyketide-CoA. Polyketone cyclization likely arises on CoA but not on the enzyme. Experimental data suggest that cyclization of linear tetraketidyl-CoA occurs in concert with or before decarboxylation of the terminal carboxyl group
Products: -
Products: -
?
4 malonyl-CoA
3,5-dihydroxyphenylacetyl-CoA + 3 CoA + 4 CO2 + H2O
-
Substrates: the enzyme is involved in biosynthesis of 3,5-dihydroxyphenylglycine, a key nonproteinogenic residue in the vancomycin family of antibiotics
Products: -
Products: -
?
4 malonyl-CoA
3,5-dihydroxyphenylacetyl-CoA + 3 CoA + 4 CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 malonyl-CoA
(3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O
Substrates: 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
Products: -
Products: -
?
4 malonyl-CoA
3,5-dihydroxyphenylacetyl-CoA + 3 CoA + 4 CO2 + H2O
-
Substrates: the enzyme is involved in biosynthesis of 3,5-dihydroxyphenylglycine, a key nonproteinogenic residue in the vancomycin family of antibiotics
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A075FAK1_AMYLU
366
0
39004
TrEMBL
other Location (Reliability: 2)
A0A193C6F1_AMYOR
366
0
39160
TrEMBL
other Location (Reliability: 2)
A0A1W2LXY0_9PSEU
366
0
38982
TrEMBL
-
A0A229R775_AMYAL
366
0
38929
TrEMBL
other Location (Reliability: 2)
A0A2P2FRG0_AMYLU
366
0
39004
TrEMBL
-
A0A2S6GUM9_9PSEU
366
0
38842
TrEMBL
Secretory Pathway (Reliability: 2)
A0A428X5T8_AMYBA
366
0
38902
TrEMBL
-
A0A428ZIW5_KIBAR
366
0
38975
TrEMBL
Secretory Pathway (Reliability: 4)
S5TLS0_9BACT
372
0
39350
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C160A
-
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
-
kcat/Km for malonyl-CoA is 2.3% compared to the kcat/Km-value of the wild-type enzyme
C160A/C190A
-
formation of (3,5-dihydroxyphenylacetyl)-CoA is barely detectable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tseng, C.C.; McLoughlin, S.M.; Kelleher, N.L.; Walsh, C.T.
Role of the active site cysteine of DpgA, a bacterial type III polyketide synthase
Biochemistry
43
970-980
2004
Amycolatopsis mediterranei
brenda
Wu, H.C.; Li, Y.S.; Liu, Y.C.; Lyu, S.Y.; Wu, C.J.; Li, T.L.
Chain elongation and cyclization in type III PKS DpgA
Chembiochem
13
862-871
2012
Amycolatopsis orientalis
brenda
Pfeifer, V.; Nicholson, G.J.; Ries, J.; Recktenwald, J.; Schefer, A.B.; Shawky, R.M.; Schrder, J.; Wohlleben, W.; Pelzer, S.
A polyketide synthase in glycopeptide biosynthesis: the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine
J. Biol. Chem.
276
38370-38377
2001
Amycolatopsis mediterranei (Q939X3)
brenda
Chen, H.; Tseng, C.C.; Hubbard, B.K.; Walsh, C.T.
Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine
Proc. Natl. Acad. Sci. USA
98
14901-14906
2001
Amycolatopsis orientalis, Amycolatopsis orientalis NRRL 18098
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.246)
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