Information on EC 2.7.8.7 - holo-[acyl-carrier-protein] synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.7.8.7
-
RECOMMENDED NAME
GeneOntology No.
holo-[acyl-carrier-protein] synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
sequential binding mechanism: initial CoA- and Mg2+-binding followed by binding of acyl-carrier protein (ACP), nucleophilic attack of ACP-serine-hydroxylate on beta-phosphate of CoA followed by charge migration, Lys185-protonation, diphosphate-cleavage, and product dissociation, rate limiting step: release of 3',5'-ADP, key acid/base catalysts: residues E181 (CoA-binding) and K185 (Mg2+-binding)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acyl carrier protein metabolism I
-
-
acyl carrier protein metabolism II (mammalian)
-
-
enterobactin biosynthesis
-
-
lipid metabolism
-
-
Pantothenate and CoA biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
CoA-[4'-phosphopantetheine]:apo-[acyl-carrier protein] 4'-pantetheinephosphotransferase
Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4'-phosphopantetheinyl transferase
-
4'-phosphopantetheinyl transferase
-
-
4'-phosphopantetheinyl transferase
-
-
4'-phosphopantetheinyl transferase
-
-
4'-phosphopantetheinyl transferase
-
4'-PP transferase
-
4-phosphopantetheinyl transferase
-
-
4-phosphopantetheinyl transferase
Bacillus subtilis ATCC 6633
-
-
-
4-phosphopantetheinyl transferase
-
-
4-phosphopantetheinyl transferase
Fusarium fujikuroi IMI58289
-
-
-
4-phosphopantetheinyl transferase
-
-
4-phosphopantetheinyl transferase
Mycobacterium tuberculosis BCG
-
-
-
4-phosphopantetheinyl transferase
-
-
4-phosphopantetheinyl transferase
-
-
AcpS
-
acyl carrier protein synthases that recognize carrier protein from primary metabolism
AcpS
Streptomyces chattanoogensis L10
-
-
AcpS
Streptomyces pneumoniae
-
-
acyl carrier protein holoprotein (holo-ACP) synthetase
-
-
-
-
acyl carrier protein synthase
-
-
acyl carrier protein synthase
-
-
acyl carrier protein synthetase
-
-
-
-
acyl carrier protein-specific 4'-phosphopantetheinyl transferase
-
-
coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine transferase
-
-
-
-
cytoplasmic type I FAS multienzyme
-
-
EntD
-
gene name
holo ACP synthase
acpS gene
holo ACP synthase
-
-
holo-ACP synthase
-
-
-
-
holo-ACP synthetase
-
-
-
-
holosynthase
-
-
-
-
human PPTase
-
-
mitochondrial type II fatty acid synthase
-
-
phosphopantetheine:protein transferase
-
-
phosphopantetheinyl transferase
-
-
phosphopantetheinyl transferase
-
-
-
phosphopantetheinyl transferase
-
-
phosphopantetheinyl transferase
-
phosphopantetheinyl transferase
-
-
phosphopantetheinyl transferase
-
close to the class two phosphopantetheinyl transferase Sfp from Bacillus subtilis
phosphopantetheinyl transferase
-
-
phosphopantetheinyl transferase
-
-
phosphopantetheinyl transferases
-
phosphopantetheinyl transferases
Streptomyces chattanoogensis L10
-
-
PPT
Streptomyces chattanoogensis L10
-
-
PPT1
Fusarium fujikuroi IMI58289
-
-
-
PPTase
Bacillus subtilis ATCC 6633
-
-
-
PPTase
Fusarium fujikuroi IMI58289
-
-
-
PPTase
Mycobacterium tuberculosis BCG
-
-
-
PPTase
Streptomyces chattanoogensis L10
-
-
PPTase
Streptomyces verticillus ATCC15003
-
-
PptB
-
isoform
PptB
-
isoform
-
PptT
Mycobacterium tuberculosis BCG
-
isoform
-
Sfp
Bacillus subtilis ATCC 6633
-
-
-
surfactin synthetase
-
-
type I rat fatty acid synthase ACP
-
-
type II fatty acid synthase system
Streptomyces pneumoniae
-
-
type-I fatty acid synthase FAS-A
-
-
CAS REGISTRY NUMBER
COMMENTARY
37278-30-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain FGSC4
-
-
Manually annotated by BRENDA team
Aspergillus nidulans FGSC4
strain FGSC4
-
-
Manually annotated by BRENDA team
Bacillus subtilis ATCC 6633
-
-
-
Manually annotated by BRENDA team
isolate ND90Pr (ATCC 201652)
UniProt
Manually annotated by BRENDA team
isoform AcpS
UniProt
Manually annotated by BRENDA team
isoform Sfp
UniProt
Manually annotated by BRENDA team
K-12 derivatives
-
-
Manually annotated by BRENDA team
strain K-12, isoform AcpT
-
-
Manually annotated by BRENDA team
Fusarium fujikuroi IMI58289
-
-
-
Manually annotated by BRENDA team
human
-
-
Manually annotated by BRENDA team
strain MP-1
-
-
Manually annotated by BRENDA team
Moritella marina MP-1
strain MP-1
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis BCG
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
strain MP4, denoted acpS1 gene
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli MP4
strain MP4, denoted acpS1 gene
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
yeast, strain lys5
-
-
Manually annotated by BRENDA team
castor-oil-seed, L. cv. Baker 296
-
-
Manually annotated by BRENDA team
strain W303; yeast
-
-
Manually annotated by BRENDA team
strain ATCC24843
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe ATCC24843
strain ATCC24843
-
-
Manually annotated by BRENDA team
spinach, L. cv. 424
-
-
Manually annotated by BRENDA team
Spinacia oleracea Melody
Melody
-
-
Manually annotated by BRENDA team
strain DW4/3-1, gene mtaA
SwissProt
Manually annotated by BRENDA team
Streptomyces chattanoogensis L10
-
UniProt
Manually annotated by BRENDA team
Streptomyces pneumoniae
-
-
-
Manually annotated by BRENDA team
Streptomyces pneumoniae
apcS gene, open reading frame starting at the second Met codon
SwissProt
Manually annotated by BRENDA team
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
Manually annotated by BRENDA team
Streptomyces verticillus ATCC15003
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
Manually annotated by BRENDA team
acpP gene
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme silencing by small interfering RNA in A-549 cells prevents FDH modification. Enzyme-silenced cells demonstrate significantly reduced proliferation and undergo strong G1 arrest
malfunction
inactivation of the enzyme abolishes production of natamycin but not the spore pigment
malfunction
-
after 18 h incubation at 37C DELTApptB spores are swollen. Some germinate, but then arrest at this stage
malfunction
-
The ppt1 deletion mutants are auxotrophic for lysine, produce nonpigmented conidia, and are unable to synthesize nonribosomal peptides. Although spore germination is severely compromised under both low and high iron availability, mycelial growth occurs faster than the wild type, and the mutants are able to efficiently colonize plant roots. The ppt1 deletion mutants are unable of inhibiting growth of phytopathogenic fungi in vitro and are defective in induction of salicylic acid-dependent defense responses in Arabidopsis thaliana
malfunction
deletion of PPT1 generates mutants that are auxotrophic for lysine, unable to synthesize melanin, hypersensitive to iron and oxidative stress (H2O2) and significantly reduced in virulence to barley cultivar Bowman
malfunction
-
deletion of the ppt1 gene results in loss of polyketide synthase- and polyketide synthase/non-ribosomal peptide synthase-derived products and in transcriptional down-regulation of distinct secondary metabolite cluster genes
malfunction
-
after 18 h incubation at 37C DELTApptB spores are swollen. Some germinate, but then arrest at this stage
-
malfunction
Fusarium fujikuroi IMI58289
-
deletion of the ppt1 gene results in loss of polyketide synthase- and polyketide synthase/non-ribosomal peptide synthase-derived products and in transcriptional down-regulation of distinct secondary metabolite cluster genes
-
malfunction
Streptomyces chattanoogensis L10
-
inactivation of the enzyme abolishes production of natamycin but not the spore pigment
-
metabolism
-
AcpS is a doubly promiscuous enzyme capable of activation of acyl-carrier proteins from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates
metabolism
-
the enzyme is essential for activation of non-ribosomal peptide synthetase and polyketide synthase enzymes
metabolism
isoform AcpS specifically modifies a stand-alone acyl carrier protein that possesses a mitochondrial import signal; isoform Sfp in contrast is specific to type I multifunctional polyketide synthase/fatty acid synthase proteins and cannot modify the stand-alone acyl carrier protein
metabolism
-
isoform Ppt1 is essentially involved in lysine biosynthesis and production of bikaverins, fusarubins and fusarins, but not moniliformin
metabolism
-
isoform PptT plays a role in the biosynthesis pathways for mycolic acids, polyketide-derived lipids and siderophores
metabolism
-
isoform AcpS specifically modifies a stand-alone acyl carrier protein that possesses a mitochondrial import signal; isoform Sfp in contrast is specific to type I multifunctional polyketide synthase/fatty acid synthase proteins and cannot modify the stand-alone acyl carrier protein
-
metabolism
Fusarium fujikuroi IMI58289
-
isoform Ppt1 is essentially involved in lysine biosynthesis and production of bikaverins, fusarubins and fusarins, but not moniliformin
-
metabolism
Mycobacterium tuberculosis BCG
-
isoform PptT plays a role in the biosynthesis pathways for mycolic acids, polyketide-derived lipids and siderophores
-
physiological function
overexpression of the enzyme not only increases the natamycin production by about 40% but also accelerates productions of both natamycin and the spore pigment
physiological function
-
the enzyme is essential for viability
physiological function
-
isoform PPT1 in plays an important role antibiosis and induction of salicylic acid and camalexin-dependent plant defense responses
physiological function
Sfp-type 4-phosphopantetheinyl transferase is required for lysine synthesis, tolerance to oxidative stress and virulence of Cochliobolus sativus on barley cultivar Bowman. Isoform PPT1 is involved in conidiation, but does not affect the size, morphology and germination of conidia
physiological function
-
isoform Ppt1 is involved in conidiation and sexual mating recognition. Isoform Ppt1 contributes to a functional iron uptake system that is controlled by the GATA-type transcription factor Sre1. Isoform Ppt1 is a pathogenicity factor in hydroponic rice cultures
physiological function
-
the enzyme is required for Mycobacterium tuberculosis growth and persistence in vivo. The enzyme is involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors in mycobacteria. The enzyme is required for the replication and survival of the tubercle bacillus during the acute and chronic phases of infection in mice
physiological function
-
the enzyme is essential for viability
-
physiological function
Fusarium fujikuroi IMI58289
-
isoform Ppt1 is involved in conidiation and sexual mating recognition. Isoform Ppt1 contributes to a functional iron uptake system that is controlled by the GATA-type transcription factor Sre1. Isoform Ppt1 is a pathogenicity factor in hydroponic rice cultures
-
physiological function
Mycobacterium tuberculosis BCG
-
the enzyme is required for Mycobacterium tuberculosis growth and persistence in vivo. The enzyme is involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors in mycobacteria. The enzyme is required for the replication and survival of the tubercle bacillus during the acute and chronic phases of infection in mice
-
physiological function
Streptomyces chattanoogensis L10
-
overexpression of the enzyme not only increases the natamycin production by about 40% but also accelerates productions of both natamycin and the spore pigment
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
-
r
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
substrate for isoform AcpS
-
?
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
substrate for isoform AcpS
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
-
r
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
recombinant enzyme
-
?
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
show the reaction diagram
substrate for isoform Sfp
-
?
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
show the reaction diagram
substrate for isoform Sfp
-
?
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
show the reaction diagram
substrate for isoform Sfp
-
?
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
show the reaction diagram
substrate for isoform Sfp
-
?
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
show the reaction diagram
substrate for isoform Sfp
-
?
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
show the reaction diagram
substrate for isoform Sfp
-
?
apo-[acyl-carrier protein] + acetyl-CoA
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
pH 7, 37C
reaction stop by 10% trichloroacetic acid, limited release of 3,5-ADP by interactions with guanidinium moieties of R74 and R86
?
benzoyl-CoA + apo-[acyl-carrier protein]
CoA + benzoyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
show the reaction diagram
-
-
-
?
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
show the reaction diagram
-
-
-
?
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
show the reaction diagram
-
-
-
?
biotin-CoA + GDSLSWLLRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRLLN + ?
show the reaction diagram
-
-
-
?
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
show the reaction diagram
-
-
-
?
biotin-CoA + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
show the reaction diagram
-
-
-
?
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
show the reaction diagram
-
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
recombinant enzyme
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
transfers 4'-phosphopantetheine from reduced coenzyme A to acyl carrier proteon apoprotein
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
Dcp from Lactobacillus casei, NodF from Rhizobium leguminosarum and several polyketide synthase ACPs from Streptomyces sp. also serves as substrates
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
Streptomycess sp. acyl carrier proteins and coenzyme A analogs also serves as substrates for holo-ACP synthase in vitro
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
functional activation of ACP in the fatty acid biosynthesis pathway, enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
enzyme Sfp required for production of the lipoheptapeptide antibiotic surfactin
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 in lysine biosynthesis
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
plays a role in polyketide biosynthesis
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
PcpS plays an essential role in both fatty acid and siderophore metabolism
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Spinacia oleracea Melody
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
functional activation of ACP in the fatty acid biosynthesis pathway, enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase, plays a role in polyketide biosynthesis
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces verticillus ATCC15003
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
show the reaction diagram
-
phosphopantetheinylation of the enzyme in volved in lysine catabolism, phosphopantetheinylation of the enzyme involved in lysine catabolism
-
r
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
show the reaction diagram
-
-
-
r
CoA + apo-[EntB-ArCP-H6 E. coli]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[fredericamycin H acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[fredericamycin acyl-carrier protein]
show the reaction diagram
-
-
?
CoA + apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[PCPH6SrfB1.18]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[PCPH6SrfB2.18]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
show the reaction diagram
Streptomyces verticillus, Streptomyces verticillus ATCC15003
-
-
r
CoA + apo-[peptidyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. frenolicin-acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[Streptomyces sp. granaticin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. granaticin-acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
show the reaction diagram
-
-
-
r
CoA + apo-[tetracenomycin M acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[tetracenomycin M acyl-carrier protein]
show the reaction diagram
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
show the reaction diagram
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis BCG
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces chattanoogensis L10
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
show the reaction diagram
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
show the reaction diagram
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
show the reaction diagram
Pseudomonas aeruginosa, Pseudomonas putida, Bacillus subtilis ATCC 6633
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[FDH protein]
adenosine 3',5'-bisphosphate + holo-[FDH protein]
show the reaction diagram
-
the enzyme modifies the apo-FDH protein at serine 354 and activates its catalysis
-
?
crotonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
decanoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
-
r
desulfoCoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
? + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
show the reaction diagram
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
myristoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
myristoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
palmitoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
palmitoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
phenylacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
-
r
additional information
?
-
-
Sfp type exhibits an extraordinarily broad substrate specificity
-
-
-
additional information
?
-
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
-
additional information
?
-
activates polyketide synthases and polypetide synthases, processes an aryl carrier protein domain ArCP, derived from the enterobactin synthetase of Escherichia coli, as well as a peptidyl carrier protein domain from a polypeptide synthase of yet unknown function from Sorangium cellulosum
-
-
-
additional information
?
-
Escherichia coli ACP and mutant ACP proteins rACP, V12G, F50A, I54L, I154V, A59G and Y71A are substrates, mutant I54A is no substrate
-
-
-
additional information
?
-
-
mutant ACP in which the target serine 36 has been mutated to a threonine residue is an inactive substrate for phosphopantetheinylation
-
-
-
additional information
?
-
-
3'-dephospho-CoA is no substrate
-
-
-
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
-
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
-
additional information
?
-
Streptomyces pneumoniae
dephospho-CoA is no substrate
-
-
-
additional information
?
-
-
single broad specificity enzyme for all posttranslational 4'-phosphopantetheinylation reactions, also capable of phosphopantetheinylation of peptidyl carrier and acyl carrier proteins from prokaryotes
-
-
-
additional information
?
-
-
SePptII is active in phosphopantetheinyl transfer with an acyl carrier protein-thioesterase didomain from the erythromycin polyketide synthase as substrate. SePptII provides complete modification of acyl-carrier protein-thioesterase and of an entire multienzymne subunit from the erythromycin polyketide synthase
-
-
-
additional information
?
-
enzyme is involved in fredericamycin biosynthesis
-
-
-
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
-
additional information
?
-
-
isoform AcpT modifies two carrier proteins encoded in O-island 138, a cluster of fatty acid biosynthesis-like genes
-
-
-
additional information
?
-
-
D35 in site A of acyl carrier protein is critical for enzyme activity
-
-
-
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
-
additional information
?
-
-
isoform PptB is unable to phosphopantetheinylate AarA protein
-
-
-
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
-
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
-
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
-
additional information
?
-
-
isoform PptB is unable to phosphopantetheinylate AarA protein
-
-
-
additional information
?
-
Streptomyces chattanoogensis L10
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
-
additional information
?
-
Streptomyces chattanoogensis L10
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
-
additional information
?
-
Streptomyces verticillus ATCC15003
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
-
additional information
?
-
Moritella marina MP-1
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Q12036
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Q9RFL1
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Q9F0Q6
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
P0A2W3
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
functional activation of ACP in the fatty acid biosynthesis pathway, enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
-
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces pneumoniae
P0A2W7
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
enzyme Sfp required for production of the lipoheptapeptide antibiotic surfactin
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 in lysine biosynthesis
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
plays a role in polyketide biosynthesis
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
PcpS plays an essential role in both fatty acid and siderophore metabolism
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Spinacia oleracea Melody
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
functional activation of ACP in the fatty acid biosynthesis pathway, enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase, plays a role in polyketide biosynthesis
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Streptomyces verticillus ATCC15003
Q9F0Q6
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
show the reaction diagram
-
phosphopantetheinylation of the enzyme involved in lysine catabolism
-
r
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
show the reaction diagram
-
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Q9NRN7
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis, Mycobacterium tuberculosis BCG
-
-
-
?
additional information
?
-
Q2MGB1
enzyme is involved in fredericamycin biosynthesis
-
-
-
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
-
additional information
?
-
-
isoform AcpT modifies two carrier proteins encoded in O-island 138, a cluster of fatty acid biosynthesis-like genes
-
-
-
additional information
?
-
Moritella marina MP-1
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4'-phosphopantetheine
prosthetic group
4'-phosphopantetheine
-
-
4'-phosphopantetheine
-
-
4'-phosphopantetheine
-
-
4'-phosphopantetheine
-
-
4'-phosphopantetheine
-
-
4'-phosphopantetheine
-
4'-phosphopantetheine
-
-
4'-phosphopantetheine
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
maximal activity at 0.025 mM
Mg2+
-
requires Mg2+ or Mn2+ for activity, Km for Mg2+ 3.0 mM
Mg2+
-
requires Mg2+ or Mn2+ for activity, Km for Mg2+ 3.0 mM
Mg2+
nonessential for binding of coenzyme A (CoA)
Mg2+
-
contains Mg2+
Mg2+
-
dependent on
Mn2+
-
requires Mn2+ or Mg2+ for activity
additional information
-
CuSO4, CdCl2 and CrCl2 does not stimulate the reaction at any ceoncentration, trivalent metal cations such as FeCl3 or AlCl3 are ineffective
additional information
-
Ca2+, Fe2+, Co2+ and Zn2+ are ineffective, inhibitory or both, at intermediate and high concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-5-fluoro-benzoic acid
-
IC50: 0.0021 mM
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.015 mM
3',5'-ADP
-
inhibited in vitro by the reaction product
3',5'-ADP
-
-
3',5'-ADP
Streptomyces pneumoniae
product inhibition
5-bromo-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0015 mM
5-bromo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0034 mM
5-bromo-4-chloro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.002 mM
5-carboxyamino-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00013 mM
5-chloro-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0011 mM
5-fluoro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0019 mM
5-iodo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0013 mM
5-methyl-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00027 mM
5-methyl-2-[[5-oxo-2-(3-trifluoromethoxy-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0044 mM
-
5-methyl-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00083 mM
-
apo-acyl-carrier protein
-
substrate inhibition
apo-acyl-carrier protein
-
-
apo-acyl-carrier protein
-
mutant ACP in which the target serine 36 has been mutated to a threonine residue is an inhibitor as well as an inactive substrate
apo-acyl-carrier protein
Streptomyces pneumoniae
slight inhibition at 0.005-0.01 mM
additional information
-
no substrate inhibition by apo-peptide(1--74)
-
additional information
-
no substantial inhibition of Sfp by apo-[PCPH6SrfB1.18]
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
apo-acyl-carrier protein
Streptomyces pneumoniae
significantly stimulating above 0.01 mM
CoA
-
stimulates the holoACP synthase reaction within the intact organelle
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0088
acetoacetyl-CoA
pH 7.5, 22C
0.019
acetoacetyl-CoA
-
pH 7.5, 22C
0.0077
acetyl-CoA
pH 7.5, 22C
0.011
acetyl-CoA
-
pH 7.5, 22C
0.0247
acetyl-CoA
+/-0.0036 mM, mutant K185A
0.0249
acetyl-CoA
+/-0.003 mM, wild-type
0.043
acetyl-CoA
-
pH 7.5, 22C
0.0454
acetyl-CoA
+/-0.0038 mM, mutant E181A
0.047
acetyl-CoA
+/-0.023 mM, mutant Q112E
0.076
acetyl-CoA
+/-0.0038 mM, mutant R47A
0.081
acetyl-CoA
+/-0.0013 mM, mutant E181Q
0.093
acetyl-CoA
+/-0.001 mM, double mutant Q112E, E181Q
0.095
acetyl-CoA
+/-0.033 mM, mutant H111A
0.142
acetyl-CoA
+/-0.035 mM, mutant D129A
0.399
acetyl-CoA
+/-0.041 mM, mutant R86A
0.017
apo-ACP
pH 7.8, 37C, mutant acyl carrier protein F50A
-
0.021
apo-ACP
-
pH 7.0, 37C, Bacillus subtilis acyl carrier protein-A as substrate
-
0.035
apo-ACP
pH 7.8, 37C, mutant ACP I54V
-
0.038
apo-ACP
-
pH 8.8, 37C, isoenzyme Sfp, 0.02-0.2 mM substrate
-
0.068
apo-ACP
-
pH 8.8, 37C, isoenzyme AcpS, 0.02-0.2 mM substrate
-
0.0002
apo-acyl-carrier protein
-
pH 8.8, 37C, isoenzyme AcpS, 0.002-0.008 mM substrate
0.0004
apo-acyl-carrier protein
-
-
0.0004
apo-acyl-carrier protein
-
pH 8.0, 33C
0.0005
apo-acyl-carrier protein
Streptomyces pneumoniae
pH 7.0, 37C
0.00055
apo-acyl-carrier protein
-
pH 8.0, 33C
0.001
apo-acyl-carrier protein
-
pH 8.8, 37C
0.0013
apo-acyl-carrier protein
Streptomyces pneumoniae
pH 7.0, 37C, trichloroacetic acid precipitation method
0.0014
apo-acyl-carrier protein
-
pH 8.8, 37C, isoenzyme Sfp, 0.002-0.008 mM substrate
0.0015
apo-acyl-carrier protein
-
pH 8.8, 37C
0.002
apo-acyl-carrier protein
-
pH 8.0, 37C
0.002
apo-acyl-carrier protein
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.003
apo-acyl-carrier protein
pH 7.8, 37C, mutant acyl carrier protein Y71A
0.0031
apo-acyl-carrier protein
-
pH 7.0, 37C, human acyl carrier protein f as as substrate
0.006
apo-acyl-carrier protein
-
pH 6.0, 37C
0.0073
apo-acyl-carrier protein
pH 7.8, 37C, mutant acyl carrier protein V12G
0.0075
apo-acyl-carrier protein
-
pH 7.0, 37C, human acyl carrier protein mit as substrate
0.0079
apo-acyl-carrier protein
pH 7.8, 37C
0.0087
apo-acyl-carrier protein
pH 7.8, 37C, r acyl carrier protein
0.0094
apo-acyl-carrier protein
pH 7.8, 37C, Escherichia coli acyl carrier protein
0.013
apo-acyl-carrier protein
pH 7.8, 37C, mutant acyl carrier protein A59G
0.029
apo-acyl-carrier protein
pH 7.8, 37C, mutant acyl carrier protein I54L
0.072
apo-acyl-carrier protein
-
pH 8.0, 37C
0.002
apo-peptide(1-->74)
-
pH 8.0, 33C
-
0.002
apo-peptide(1-->74)
-
-
-
0.00445
apo-peptidyl carrier protein
-
pH 8.8, 37C, isoenzyme Sfp
0.0064
apo-peptidyl carrier protein
-
pH 7.0, 37C
0.0216
apo-peptidyl carrier protein
-
pH 8.8, 37C, isoenzyme AcpS, apo-hPCP
0.026
apo-peptidyl carrier protein
-
pH 8.8, 37C, isoenzyme Sfp, apo-hPCP
0.0008
apo-[acyl-carrier protein]
-
pH 7.5, 22C
0.0013
apo-[acyl-carrier protein]
pH 7.5, 22C
0.0018
apo-[acyl-carrier protein]
-
pH 7.5, 22C
0.0033
apo-[BpsA protein]
-
in 100 mM Tris-HCl, pH 7.8, at 30C
-
0.0065
apo-[BpsA protein]
-
in 100 mM Tris-HCl, pH 7.8, at 30C
-
0.0086
apo-[BpsA protein]
-
in 100 mM Tris-HCl, pH 7.8, at 30C
-
0.016
apo-[EntB-ArCP-H6 Escherichia coli]
-
pH 6.0, 37C
-
0.0058
apo-[fredericamycin H acyl-carrier protein]
pH 8.0, 37C
0.005
apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
-
pH 6.0, 37C
-
0.0018
apo-[PCPH6SrfB2.18]
-
pH 6.0, 37C
-
0.0031
apo-[peptidyl carrier protein]
pH 8.0, 37C
0.0039
apo-[peptidyl carrier protein]
pH 8.0, 37C
0.012
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.005
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.039
apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.022
apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.1
apo-[tetracenomycin M acyl-carrier protein]
pH 8.0, 37C
0.007
Butyryl-CoA
-
pH 7.5, 22C
0.0081
Butyryl-CoA
pH 7.5, 22C
0.035
Butyryl-CoA
-
pH 7.5, 22C
0.004
CoA
-
pH 7.5, 22C
0.007
CoA
-
pH 6.0, 37C
0.0071
CoA
Streptomyces pneumoniae
pH 7.0, 37C, trichloroacetic acid precipitation method
0.0093
CoA
pH 7.5, 22C
0.0115
CoA
Streptomyces pneumoniae
pH 7.0, 37C
0.04
CoA
-
pH 7.5, 22C
0.05
CoA
-
pH 8.8, 37C
0.15
CoA
-
pH 8.0, 33C
0.00062
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30C
0.0038
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30C
0.011
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30C
0.0052
crotonyl-CoA
-
pH 7.5, 22C
0.018
crotonyl-CoA
-
pH 7.5, 22C
0.0014
decanoyl-CoA
-
pH 7.5, 22C
0.0015
decanoyl-CoA
-
pH 7.5, 22C
0.123
DSLEFIASKLA
-
-
0.242
DSLEFIASKLA
-
-
0.117
GDSLDMLEWSLM
-
-
0.534
GDSLDMLEWSLM
-
-
0.108
GDSLSWLLRCLN
-
-
0.12
GDSLSWLLRCLN
-
-
0.0515
GDSLSWLLRLLN
-
-
0.076
GDSLSWLLRLLN
-
-
0.221
GDSLSWLLRSLN
-
-
0.254
GDSLSWLLRSLN
-
-
0.0772
GDSLSWLVRCLN
-
-
0.139
GDSLSWLVRCLN
-
-
0.0618
GDSLSWLVRLLN
-
-
0.105
GDSLSWLVRLLN
-
-
0.0071
malonyl-CoA
pH 7.5, 22C
0.015
malonyl-CoA
-
pH 7.5, 22C
0.44
Mg2+
+/-0.04 mM, wild-type
0.75
Mg2+
+/-0.24 mM, mutant Q112E
1.1
Mg2+
+/-0.1 mM, mutant K185A
3.3
Mg2+
+/-1 mM, mutant R47A
4.6
Mg2+
+/-0.3 mM, mutant D129A
7.6
Mg2+
+/-4.6 mM, mutant E181Q
15
Mg2+
+/-3 mM, mutant R86A
18.3
Mg2+
+/-0.7 mM, mutant E181A
34.5
Mg2+
+/-5.6 mM, mutant H111A
0.0025
myristoleoyl-CoA
-
pH 7.5, 22C
0.001
myristoyl-CoA
-
pH 7.5, 22C
0.0018
myristoyl-CoA
-
pH 7.5, 22C
0.0009
palmitoleoyl-CoA
-
pH 7.5, 22C
0.0016
palmitoleoyl-CoA
-
pH 7.5, 22C
0.0012
palmitoyl-CoA
-
pH 7.5, 22C
0.051
acetoacetyl-CoA
-
pH 7.5, 22C
additional information
acetyl-CoA
double mutant Q112E, E181Q, Kcat/KM: 0.2 1/min/mM; mutant D129A, Kcat/KM: 0.04 1/min/mM; mutant E181A, Kcat/KM: 0.9 1/min/mM; mutant E181Q, Kcat/KM: 0.5 1/min/mM; mutant H111A, Kcat/KM: 64.2 1/min/mM; mutant K185A, Kcat/KM: 0.6 1/min/mM; mutant Q112E, Kcat/KM: 46.8 1/min/mM; mutant R47A, Kcat/KM: 447 1/min/mM; mutant R86A, Kcat/KM: 146 1/min/mM; wild-type, Kcat/KM: 578 1/min/mM
0.094
malonyl-CoA
-
pH 7.5, 22C
additional information
Mg2+
mutant D129A, Kcat/KM: 0.0001 1/min/mM; mutant E181A, Kcat/KM: 0.001 1/min/mM; mutant E181Q, Kcat/KM: 0.005 1/min/mM; mutant H111A, Kcat/KM: 0.21 1/min/mM; mutant K185A, Kcat/KM: 0.016 1/min/mM; mutant Q112E, E181Q, Kcat/KM: 0.0002 1/min/mM; mutant Q112E, Kcat/KM: 1.76 1/min/mM; mutant R47A, Kcat/KM: 14.5 1/min/mM; mutant R86A, Kcat/KM: 4.8 1/min/mM; wild-type, Kcat/KM: 32.7 1/min/mM
104.1
Mg2+
+/-51 mM, double mutant Q112E, E181Q
additional information
additional information
-
KM-values numbers with mutants of peptidyl-carrier protein as substrate
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
acetoacetyl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.2
acetoacetyl-CoA
Escherichia coli
P24224
pH 7.5, 22C
0.2
acetoacetyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.000098
acetyl-CoA
Homo sapiens
Q9NRN7
mutant D129A
0.00025
acetyl-CoA
Homo sapiens
Q9NRN7
mutant K185A
0.0004
acetyl-CoA
Homo sapiens
Q9NRN7
double mutant Q112E, E181Q
0.00072
acetyl-CoA
Homo sapiens
Q9NRN7
mutant E181A
0.00073
acetyl-CoA
Homo sapiens
Q9NRN7
mutant E181Q
0.009
acetyl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.037
acetyl-CoA
Homo sapiens
Q9NRN7
mutant Q112E
0.102
acetyl-CoA
Homo sapiens
Q9NRN7
mutant H111A
0.2
acetyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.24
acetyl-CoA
Homo sapiens
Q9NRN7
wild-type
0.4
acetyl-CoA
Escherichia coli
P24224
pH 7.5, 22C
0.57
acetyl-CoA
Homo sapiens
Q9NRN7
mutant R47A
0.973
acetyl-CoA
Homo sapiens
Q9NRN7
mutant R86A
0.0283
apo-acyl-carrier protein
Bacillus subtilis
-
pH 8.8, 37C, isoenzyme Sfp, 0.002-0.008 mM substrate
0.0967
apo-acyl-carrier protein
Bacillus subtilis
-
pH 6.0, 33C
0.208
apo-acyl-carrier protein
Bacillus subtilis
-
pH 8.8, 37C, isoenzyme Sfp, 0.02-0.2 mM substrate
0.367
apo-acyl-carrier protein
Bacillus subtilis
-
pH 8.8, 37C, isoenzyme AcpS, 0.002-0.008 mM substrate
1.03
apo-acyl-carrier protein
Escherichia coli
-
pH 8.8, 37C, 250 mM NaCl
1.08
apo-acyl-carrier protein
Escherichia coli
-
pH 8.8, 37C
1.17
apo-acyl-carrier protein
Escherichia coli
-
pH 8.8, 37C
1.33 - 1.67
apo-acyl-carrier protein
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
1.7
apo-acyl-carrier protein
Bacillus subtilis
-
pH 6.0, 37C
2.08
apo-acyl-carrier protein
Bacillus subtilis
-
pH 8.8, 37C, isoenzyme AcpS, 0.02-0.2 mM substrate
0.239
apo-peptidyl carrier protein
Bacillus subtilis
-
pH 8.8, 37C, isoenzyme AcpS, apo-hPCP
1.6
apo-peptidyl carrier protein
Bacillus subtilis
-
pH 8.8, 37C, isoenzyme Sfp; pH 8.8, 37C, isoenzyme Sfp, apo-hPCP
0.002
apo-[acyl-carrier protein]
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.6
apo-[acyl-carrier protein]
Streptococcus pneumoniae
-
pH 7.5, 22C
0.7
apo-[acyl-carrier protein]
Escherichia coli
P24224
pH 7.5, 22C
0.035
apo-[BpsA protein]
Bacillus subtilis
-
in 100 mM Tris-HCl, pH 7.8, at 30C
-
0.183
apo-[BpsA protein]
Pseudomonas putida
-
in 100 mM Tris-HCl, pH 7.8, at 30C
-
0.683
apo-[BpsA protein]
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl, pH 7.8, at 30C
-
1.08
apo-[EntB-ArCP-H6 Escherichia coli]
Bacillus subtilis
-
pH 6.0, 37C
-
0.75
apo-[fredericamycin H acyl-carrier protein]
Streptomyces griseus
Q2MGB1
pH 8.0, 37C
0.95
apo-[fredericamycin H acyl-carrier protein]
Streptomyces griseus
Q2MGB1
pH 8.0, 37C
1.17
apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
Bacillus subtilis
-
pH 6.0, 37C
-
1.73
apo-[PCPH6SrfB1.18]
Bacillus subtilis
-
pH 6.0, 37C
-
0.933
apo-[PCPH6SrfB2.18]
Bacillus subtilis
-
pH 6.0, 37C
-
0.183
apo-[peptidyl carrier protein]
Streptomyces verticillus
Q9F0Q6
pH 8.0, 37C, substrate BlmI
1.43
apo-[peptidyl carrier protein]
Streptomyces verticillus
Q9F0Q6
pH 8.0, 37C, substrate TcmM
0.317
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.5
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.167
apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.09
apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.004
Butyryl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.2
Butyryl-CoA
Escherichia coli
P24224
pH 7.5, 22C
0.3
Butyryl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.002
CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.3
CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
1
CoA
Escherichia coli
P24224
pH 7.5, 22C
2.8
CoA
Pseudomonas aeruginosa
-
-
0.0027
CoA-[4'-phosphopantetheine]
Bacillus subtilis
-
in 100 mM Tris-HCl, pH 7.8, at 30C
0.037
CoA-[4'-phosphopantetheine]
Pseudomonas putida
-
in 100 mM Tris-HCl, pH 7.8, at 30C
0.075
CoA-[4'-phosphopantetheine]
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl, pH 7.8, at 30C
0.005
crotonyl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.2
crotonyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.004
decanoyl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.5
decanoyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.013
DSLEFIASKLA
Escherichia coli
-
-
0.18
DSLEFIASKLA
Bacillus subtilis
-
-
0.004
GDSLDMLEWSLM
Bacillus subtilis
-
-
0.03
GDSLDMLEWSLM
Escherichia coli
-
-
0.001
GDSLSWLLRCLN
Escherichia coli
-
-
0.17
GDSLSWLLRCLN
Bacillus subtilis
-
-
0.0005
GDSLSWLLRLLN
Escherichia coli
-
-
0.17
GDSLSWLLRLLN
Bacillus subtilis
-
-
0.0013
GDSLSWLLRSLN
Escherichia coli
-
-
0.14
GDSLSWLLRSLN
Bacillus subtilis
-
-
0.0007
GDSLSWLVRCLN
Escherichia coli
-
-
0.07
GDSLSWLVRCLN
Bacillus subtilis
-
-
0.0005
GDSLSWLVRLLN
Escherichia coli
-
-
0.05
GDSLSWLVRLLN
Bacillus subtilis
-
-
0.0004
malonyl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.1
malonyl-CoA
Escherichia coli
P24224
pH 7.5, 22C
0.1
malonyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.0003
Mg2+
Homo sapiens
Q9NRN7
mutant K185A
0.00032
Mg2+
Homo sapiens
Q9NRN7
double mutant Q112E, E181Q
0.00038
Mg2+
Homo sapiens
Q9NRN7
mutant E181A
0.00065
Mg2+
Homo sapiens
Q9NRN7
mutant E181Q
0.0007
Mg2+
Homo sapiens
Q9NRN7
mutant D129A
0.022
Mg2+
Homo sapiens
Q9NRN7
mutant Q112E
0.122
Mg2+
Homo sapiens
Q9NRN7
mutant H111A
0.24
Mg2+
Homo sapiens
Q9NRN7
wild-type
0.8
Mg2+
Homo sapiens
Q9NRN7
mutant R47A
0.5
myristoleoyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.003
myristoyl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.5
myristoyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.003
palmitoleoyl-CoA
Mycoplasma pneumoniae
-
pH 7.5, 22C
0.4
palmitoleoyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.4
palmitoyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
1.2
Mg2+
Homo sapiens
Q9NRN7
mutant R86A
additional information
additional information
Bacillus subtilis
-
turnover numbers with mutants of peptidyl-carrier protein as substrate
-
additional information
additional information
Pseudomonas aeruginosa
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.7
apo-[BpsA protein]
Pseudomonas putida
-
in 100 mM Tris-HCl, pH 7.8, at 30C
12240
107
apo-[BpsA protein]
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl, pH 7.8, at 30C
12240
108
apo-[BpsA protein]
Bacillus subtilis
-
in 100 mM Tris-HCl, pH 7.8, at 30C
12240
3.3
CoA-[4'-phosphopantetheine]
Pseudomonas putida
-
in 100 mM Tris-HCl, pH 7.8, at 30C
6985
3.5
CoA-[4'-phosphopantetheine]
Bacillus subtilis
-
in 100 mM Tris-HCl, pH 7.8, at 30C
6985
20
CoA-[4'-phosphopantetheine]
Pseudomonas aeruginosa
-
in 100 mM Tris-HCl, pH 7.8, at 30C
6985
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
3',5'-ADP
Streptomyces pneumoniae
pH 7.0, 37C
0.00042
6-nitroso-1,2-benzopyrone
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.00053
6-nitroso-1,2-benzopyrone
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.0024
6-nitroso-1,2-benzopyrone
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.003
6-nitroso-1,2-benzopyrone
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.003
6-nitroso-1,2-benzopyrone
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.0052
6-nitroso-1,2-benzopyrone
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.002
apo-acyl-carrier protein
-
pH 7.0, 37C, E. coli ACP
0.054
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
pH 7.0, 37C, E. coli ACP
0.0006
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
pH 7.0, 37C, E. coli ACP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0021
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-5-fluoro-benzoic acid
Bacillus subtilis
-
IC50: 0.0021 mM
0.015
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.015 mM
0.0015
5-bromo-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0015 mM
0.0034
5-bromo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0034 mM
0.002
5-bromo-4-chloro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.002 mM
0.00013
5-carboxyamino-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00013 mM
0.0011
5-chloro-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0011 mM
0.0019
5-fluoro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0019 mM
0.0013
5-iodo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0013 mM
0.00027
5-methyl-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00027 mM
0.0044
5-methyl-2-[[5-oxo-2-(3-trifluoromethoxy-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0044 mM
-
0.00083
5-methyl-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00083 mM
-
0.0021
6-nitroso-1,2-benzopyrone
Bacillus subtilis
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.0037
6-nitroso-1,2-benzopyrone
Pseudomonas putida
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.004
6-nitroso-1,2-benzopyrone
Pseudomonas aeruginosa
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.0091
6-nitroso-1,2-benzopyrone
Bacillus subtilis
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.0098
6-nitroso-1,2-benzopyrone
Pseudomonas putida
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
0.0108
6-nitroso-1,2-benzopyrone
Pseudomonas aeruginosa
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0012
-
wild-type
0.32
-
recombinant Escherichia coli BL21(DE3)pDPJ
0.32
-
recombinant Escherichia coli BL21(DE3)pACPS1
0.32
-
recombinant apo-enzyme, expressed in Escherichia coli DH5alpha
additional information
-
specific activity 88.0 units/mg protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
Streptomyces pneumoniae
-
6.5
-
activity with apo-[acyl-carrier protein]
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
-
less than 20% of maximum activity at both pH 5.0 and 7.0, 50% of activity maximum at pH 5.5 and pH 6.8
5 - 7
-
pH 5: less than 27% of maximal activity, pH 7: less than 62% of maximal activity, activity with apo-[acyl-carrier protein]
6 - 11
-
about 20% of activity maximum at pH 6.5, about 30% of activity maximum at pH 11.0
7 - 8.8
-
half maximal activity at pH 7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 50
Streptomyces pneumoniae
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.25
-
calculated from molar extinction coefficient by the method of Gill and von Hippel
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium ulcerans (strain Agy99)
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13390
Streptomyces pneumoniae
AcpS, calculated from predicted amino acid sequence; AcpS, mass spectrometric analysis
645408
20320
mitochondrial isoenzyme, calculated from open reading frame
645405
21000
mitochondrial isoenzyme, SDS-PAGE
645405
26830
calculated from amino acid sequence of His6-tagged svp
645412
27000
-
C-terminal His6-tag fusion protein, gel filtration
662122
28000
-
-
645399
28000
-
gel filtration
645402
29000
gel fitlration
674285
29000
-
gel fitlration
674285
31600
gel filtration
645412
38000
Streptomyces pneumoniae
purified AcpS, gel filtration
645408
39000
Streptomyces pneumoniae
AcpS, sedimentation analysis
645408
41000
Streptomyces pneumoniae
AcpS, native homotrimer, predicted from nucleotide sequence
645408
50000
-
gel filtration, sucrose density gradient sedimentation
645395
53000
Streptomyces pneumoniae
gel filtration
645408
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 33460, calculated, x * 33000, SDS-PAGE
?
x * 59807, calculated, x * 60000, SDS-PAGE
?
-
x * 35000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 16800, native enzyme, calculated from amino acid sequence; x * 79600, His-tagged NusA-PptB fusion protein, SDS-PAGE
?
x * 20000, isoform AcpS, calculated from amino acid sequence; x * 27000, isoform AcpS, SDS-PAGE; x * 34000, isoform Sfp, calculated from amino acid sequence; x * 34000, isoform Sfp, SDS-PAGE
?
-
x * 16800, native enzyme, calculated from amino acid sequence; x * 79600, His-tagged NusA-PptB fusion protein, SDS-PAGE
-
?
-
x * 20000, isoform AcpS, calculated from amino acid sequence; x * 27000, isoform AcpS, SDS-PAGE; x * 34000, isoform Sfp, calculated from amino acid sequence; x * 34000, isoform Sfp, SDS-PAGE
-
?
Moritella marina MP-1
-
x * 33460, calculated, x * 33000, SDS-PAGE
-
dimer
2 * 15000, SDS-PAGE
dimer
-
2 * 15000, SDS-PAGE
homodimer
-
2 * 14000, SDS-PAGE
homodimer
-
2 * 14053, calculated from nucleotide sequence; 2 * 18470, calculated from molar extinction coefficient by the method of Gill and von Hippel
monomer
1 * 31000, SDS-PAGE
monomer
-
isoenzyme AcpS
monomer
-
-
monomer
Streptomyces verticillus ATCC15003
-
1 * 31000, SDS-PAGE
-
trimer
Streptomyces pneumoniae
-
-
trimer
Streptomyces pneumoniae
3 * 10400, homotrimer, SDS-PAGE; 3 * 13390, homotrimer, mass spectrometric analysis
trimer
-
isoenzyme Sfp
trimer
-
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-crystallized with CoA and ACP
-
apo-PPT (PDB: 2BYD) or in complex with coenzyme A (CoA, 5 mM) and Mg2+ (20 mM) (PDB: 2C43) or coenzyme A (2.5 mM) and acyl-carrier protein (S2156A mutant of ACP domain of fatty acid synthase) (PDB: 2CG5), precipitant: 14% PEG3350 and 0.05 M H3Cit/Na3Cit pH 5.7 or 2 M NaCl and 10% PEG6000 (complexes), apo-PPT: space group: P2(1)2(1)2(1), unit cell parameters: a: 63.78, b: 69.95, c: 71.24, alpha/beta fold with pseudo 2fold symmetry, N-terminal beta sheet (residues 91-116) connected to C-terminal beta sheet (residues 207-239) by a one residue linker and unique N-terminal and C-terminal extensions of 13 and 52 amino acids, respectively, PPT-CoA complex: space group: P2(1)2(1)2(1), unit cell parameters: a: 65.59, b: 68.96, c: 70.75, CoA-binding at the interface of N- and C-terminal domain mediated by PPT residues 47, 86, 110, 111, 185 (hydrophobic interactions, hydrogen bonds and salt bridges), and independent of Mg2+, Mg2+ bound through PPT residues 181 and 129 and coordinated by a water molecule, PPT-CoA-ACP complex: space group: P3(2)21, unit cell parameters: a, b: 69.36, c: 184.7, ACP-binding in the cleft between N- and C-terminal domain causes their rotation and slight closure, and is facilitated predominantly by hydrophobic interactions with PPT residues 51-54, 191, 144-148, 173, and 177 and a few polar interactions, disorder of C-terminal coil (residues 290-305), lack of Mg2+
crystallized by vapour-diffusion method, crystals belong to space group R3, with unit cell parameters a = b = 68.53, c = 85.9 A
-
hanging-drop vapor-diffusion method
-
complexed with CoA and acetyl-CoA, and mutant enzymes H110A and D111A, vapor diffusion method. Crystals of the AcpS-CoA-Mg2+ complex are obtained at 18C, from 0.3 M potassium thiocyanate (KSCN), 0.1 M sodium cacodylate (NaCac) (pH 6.5), and 15% (w/v) PEG 4000. The best diffracting crystal of the AcpS-acetyl-CoA complex is obtained in 0.2 M lithium sulfate, 25% (w/v) PEG 2000 MME, and 0.1 M NaCac (pH 6.5), in the presence of 5 mM acetyl-CoA. The D111A mutant crystallizes in 0.2 M KSCN, 0.1 M NaCac (pH 6.5), 8% (w/v) PEG 20000, and 8% (w/v) PEG 550 MME. The H110A mutant crystal is obtained in 0.3 Ms odium acetate, 0.1 M NaCac (pH 6.5), and 25% (w/v) PEG 2000 MME
-
-
Streptomyces pneumoniae
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 65
Streptomyces pneumoniae
stable in this range
645408
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable when CoA is present at half-saturating concentrations
-
very unstable, markedly protected from inactivation by the presence of half-saturating concentrations of reduced CoA
-
quite heat labile, unstable during chromatographic procedures intended for its purification, can only be partially overcome by Mg2+ and dithiothreitol, addition of ethylene glycol, glycerol, EDTA or proteinase inhibitors failed to stabilize the plant enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196C, stored in liquid nitrogen, enzyme maintains full activity for at least 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Sephadex G-25 gel filtration
-
AcpS mutant enzymes
-
Ni-NTA column chromatography
-
recombinant enzyme, expressed in Escherichia coli MV1190/pUC8-Sfp
-
recombinant isoenzymes AcpS and Sfp, expressed in Escherichia coli
-
recombinant enzyme, expressed in Escherichia coli DH5alpha
-
Ni-NTA column chromatography; Ni-NTA column chromatography
partially
-
recombinant enzyme
recombinant enzyme, expressed in Escherichia coli BL21(DE3)pACPS1
-
from bacterial lysate by immobilized metal affinity chromatography followed by gel filtration chromatography on Superdex200 HiLoad 26/60 column and concentration to 20 mg/ml or anion exchange chromatography and dialysis
amylose affinity column chromatography
-
recombinant enzyme
-
Ni-NTA column chromatography
-
recombinant C-terminal His6-tag fusion protein
-
Ni-NTA column chromatography
-
recombinant enzyme, expressed in Escherichia coli
-
purified as fatty acid synthetase complex
-
recombinant enzyme
-
recombinant enzyme
-
Ni-NTA agarose column chromatography; Ni-NTA agarose column chromatography
Ni2+ affinity column chromatography and Superdex 75 gel filtration
-
recombinant enzyme
Streptomyces pneumoniae
recombinant enzyme, expressed in Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from genomic DNA in pET23 for expression with C-terminal hexa-His tag and binding studies with Vibrio fischeri holo-ACP
expressed in Escherichia coli BL21(DE3) cells
-
PPtase gene npgA complements the lys5 deletion in Saccharomyces cerevisiae
-
cloned in Escherichia coli DH5alpha and overexpressed in Escherichia coli MV1190/pUC8-Sfp
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli, mutant enzymes
-
PPTase gene Sfp and Gsp complemented the lys5 deletion in Saccharomyces cerevisiae
-
sfp and acpS cloned and overproduced in Escherichia coli M15
-
PPTase gene gsp complemented the lys5 deletion in Saccharomyces cerevisiae
-
PPT1 cloned and expressed in Escherichia coli DH5alpha
-
CpSFP-PPT is expressed from an artificially synthesized gene with codon usage optimized for Escherichia coli
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
gene acpP cloned and overproduced from recombinant Escherichia coli BL21(DE3)pDPJ
-
gene acpS cloned and expressed in Escherichia coli BL21(DE3)
-
recombinant ACP synthase overproduced in Escherichia coli BL21(DE3)pACPS1
-
expressed in Escherichia coli BL21(DE3) cells
-
cloned and expressed in Sf9 insect cells
-
expressed in Escherichia coli BL21(DE3)-codon plus cells
-
in pCOEX1 for expression with TEV protease-cleavable N-terminal hexa-His-tag in Escherichia coli BL21(DE3)-R3
expressed in Escherichia coli BL21(DE3)DELTAentD cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
overexpression as a C-terminal His6-tag fusion protein in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
region from the rat FAS including putative acyl carrier protein cloned and overexpressed in Escherichia coli strains DH5alpha and BL21(DE3)
-
open reading frame YPL148C is the potential mitochondrial PPTase gene, expressed in Escherichia coli and Saccharomyces cerevisiae
expression in Escherichia coli
-
PPtase gene q10474, the putative lys7 gene, complements the lys5 deletion in Saccharomyces cerevisiae
-
mtaA gene of myxothiazol biosyntheic gene cluster, heterlogous coexpression with an acyl carrier protein domain in Escherichia coli XL1blue
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
acpP gene cloned, sequenced and expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
; genes acpS and acpP cloned and overexpressed in Escherichia coli, acpS complements an Escherichia coli mutant
Streptomyces pneumoniae
sequenced
Streptomyces pneumoniae
-
svp gene cloned into pQE-70 and overproduced in Escherichia coli M15(pREP4)
acpP gene amplified from a genomic Vibrio harveyi library by PCR, cloned and transformed in to Escherichia coli Bl-21
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D107A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
D107E
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
E151A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G105A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G105D
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G113Q
-
site-directed mutagenesis
I5R
-
site-directed mutagenesis
K155A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
K44A
-
mutant enzyme exhibits catalytic efficiencies that are diminished by factor 500 compared to wild-type enzyme
Q113R
-
site-directed mutagenesis
R14A
-
mutant enzyme exhibits catalytic efficiencies that are diminished by factor 500 compared to wild-type enzyme
W147A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
D129A
reduced Mg2+ affinity and catalytic efficiency, D129 plays a role in Mg2+-coordination
E181A
significant loss in enzyme activity, reduced Mg2+ affinity and catalytic efficiency
E181Q
significant loss in enzyme activity, reduced Mg2+ affinity (20fold) and catalytic efficiency (300fold)
K185
significant loss in enzyme activity, reduced catalytic efficiency
Q112E
slightly reduced catalytic efficiency
Q112E, E181Q
double mutant, reduced Mg2+ affinity (200fold) and catalytic efficiency
R47A
reduced coenzymeA and Mg2+ affinity, increased catalytic efficiency
R86A
reduced coenzymeA and Mg2+ affinity, increased catalytic efficiency
D111A
-
active site mutant exhibiting 5% of wild type activity
E57A
-
active site mutant without any activity
H110A
-
active site mutant exhibiting 28% of wild type activity
W147F
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
additional information
-
isoform AcpT cannot functially replace isoform AcpS. However, in the absence of AcpS activity, isoform AcpT allows very slow growth
R15A
-
active site mutant exhibiting 15% of wild type activity
additional information
enzyme inactivation mutant shows 93% reduction in fredericamycin synthesis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
identification of short peptide tags of 12 residues as efficient substrate for site-specific protein labeling catalyzed by enzyme
analysis
-
enzyme can be utilized in an assay for apo-ACP in biological material
biotechnology
-
identification of short peptide tags of 12 residues as efficient substrate for site-specific protein labeling catalyzed by enzyme
molecular biology
insights in molecular architecture and reaction mechanism of group II PPTs in contrast to group I PPTs (bacterial) enable screening for antibacterial agents which specifically inhibit bacterial PPTs
medicine
-
isoform PptT is a target for anti-tuberculosis drugs
medicine
Mycobacterium tuberculosis BCG
-
isoform PptT is a target for anti-tuberculosis drugs
-
molecular biology
MtaA should be a usefool tool for activating heterologously expressed polyketide synthase and nonribosomal polyketide synthase systems
medicine
Streptomyces pneumoniae
-
enzyme plays an important role in bacterial fatty acid and lipid biosynthesis, making it an attractive target for therapeutic intervention, drug design by identifying inhibitors with potential antibacterial activity
medicine
producer of the hybrid peptide-polyketide antitumor drug bleomycin
medicine
Streptomyces verticillus ATCC15003
-
producer of the hybrid peptide-polyketide antitumor drug bleomycin
-
biotechnology
mutant ACPs will be valuable in dissecting the structure-function relationships of ACP and its participation in synthesis and regulation of fatty acid, phospholipids, and other products of medical and biotechnological importance