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Information on EC 2.3.1.235 - tetracenomycin F2 synthase and Organism(s) Streptomyces glaucescens and UniProt Accession P16538

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.235 tetracenomycin F2 synthase
IUBMB Comments
A multi-domain polyketide synthase involved in the synthesis of tetracenomycin in the bacterium Streptomyces glaucescens. It involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN). A malonyl-CoA molecule is initially bound to the acyl carrier protein and decarboxylated to form an acetyl starter unit. Additional two-carbon units are added from nine more malonyl-CoA molecules.
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Streptomyces glaucescens
UNIPROT: P16538
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Word Map
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The taxonomic range for the selected organisms is: Streptomyces glaucescens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
10
malonyl-CoA
=
tetracenomycin F2
+
10
CoA
+
10
CO2
+
2
H2O
10
=
+
10
+
10
+
2
Synonyms
type ii polyketide synthase, tcm f2, tcm pks, tcmn polyketide cyclase, tcmk protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TcmK protein
the multi-domain polyketide synthase involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN)
TCM PKS
TcmN polyketide cyclase
the multi-domain polyketide synthase involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN)
type II polyketide synthase
-
-
SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:acetate malonyltransferase (tetracenomycin F2 forming)
A multi-domain polyketide synthase involved in the synthesis of tetracenomycin in the bacterium Streptomyces glaucescens. It involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN). A malonyl-CoA molecule is initially bound to the acyl carrier protein and decarboxylated to form an acetyl starter unit. Additional two-carbon units are added from nine more malonyl-CoA molecules.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10 malonyl-CoA
tetracenomycin F2 + 10 CoA + 10 CO2 + 2 H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
10 malonyl-CoA
tetracenomycin F2 + 10 CoA + 10 CO2 + 2 H2O
show the reaction diagram
-
the multi-domain polyketide synthase involved in the synthesis of tetracenomycin
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the multi-domain polyketide synthase (TcmK) involves a ketosynthase complex (TcmKL), an acyl carrier protein (TcmM), a malonyl CoA:ACP acyltransferase (MAT), and a cyclase (TcmN)
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the multi-domain polyketide synthase involved in the synthesis of tetracenomycin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KAS1_STRGA
426
0
45077
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the TcmKL KS alphabeta ketosynthase complex, an acyl carrier protein TcmM ACP, TcmN cyclase, and FabD malonyl CoA:ACP acyltransferase proteins constitute the minimal requirements for a functional tetracenomycin polyketide synthase in vitro
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C173A
plasmids carrying the C173A mutation produce no detectable amount of tetracenomycin F2
C173S
plasmids carrying the C173S mutation produce no detectable amount of tetracenomycin F2
H350L/S351A
plasmids carrying the H350L/S351A double mutation produce no detectable amount of tetracenomycin F2
S351A
plasmids carrying the S351A mutation produce high amounts of tetracenomycin F2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the TcmK/TcmL alphabeta complex
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TcmN polyketide cyclase
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of tcmN in Escherichia coli
overexpression of the tcmKL genes together in Streptomyces lividans to obtain the KS subunits
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bao, W.; Wendt-Pienkowski, E.; Hutchinson, C.R.
Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis
Biochemistry
37
8132-8138
1998
Streptomyces glaucescens
Manually annotated by BRENDA team
Meurer, G.; Hutchinson, C.R.
Functional analysis of putative beta-ketoacyl:acyl carrier protein synthase and acyltransferase active site motifs in a type II polyketide synthase of Streptomyces glaucescens
J. Bacteriol.
177
477-481
1995
Streptomyces glaucescens (P16538), Streptomyces glaucescens
Manually annotated by BRENDA team
Shen, B.; Hutchinson, C.R.
Deciphering the mechanism for the assembly of aromatic polyketides by a bacterial polyketide synthase
Proc. Natl. Acad. Sci. USA
93
6600-6604
1996
Streptomyces glaucescens (P16559), Streptomyces glaucescens
Manually annotated by BRENDA team