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Information on EC 3.1.4.14 - [acyl-carrier-protein] phosphodiesterase and Organism(s) Escherichia coli and UniProt Accession P21515

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.14 [acyl-carrier-protein] phosphodiesterase
IUBMB Comments
The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier protein (ACP) and short-chain ACPs over the medium- and long-chain species . Deletion of the gene encoding this enzyme abolishes ACP prosthetic-group turnover in vivo . Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7, holo-[acyl-carrier-protein] synthase.
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This record set is specific for:
Escherichia coli
UNIPROT: P21515
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
acyl carrier protein phosphodiesterase, acp phosphodiesterase, 4'-phosphopantetheine hydrolase, acp hydrolyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACP hydrolyase
-
acyl carrier protein phosphodiesterase
-
ACP hydrolase
-
-
ACP phosphodiesterase
-
-
acyl carrier protein phosphodiesterase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
holo-[acyl-carrier protein] 4'-pantetheine-phosphohydrolase
The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier protein (ACP) and short-chain ACPs over the medium- and long-chain species [3]. Deletion of the gene encoding this enzyme abolishes ACP prosthetic-group turnover in vivo [3]. Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7, holo-[acyl-carrier-protein] synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-21-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-carrier-protein + H2O
4'-phosphopantetheine + apo-[acyl-carrier-protein]
show the reaction diagram
-
-
-
?
acyl-carrier protein + H2O
4'-phosphopantetheine + apoprotein
show the reaction diagram
Clostridium butyricum acyl-carrier protein + H2O
4'-phosphopantetheine + apoprotein acyl-carrier protein
show the reaction diagram
-
-
-
-
?
E. coli acyl-carrier protein + H2O
4'-phosphopantetheine + apoprotein of acyl-carrier protein
show the reaction diagram
ethyldethia-acyl-carrier protein + H2O
? + apoprotein
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
AcpH readily removes the N-pentylpantothenamide-modified prosthetic group of acyl carrier proteinboth in vivo and in vitro
-
-
?
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
acyl-carrier protein + H2O
4'-phosphopantetheine + apoprotein
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
required, or other divalent cations
Fe2+
-
required, or other divalent cations
Zn2+
-
required, or other divalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
required
dithiothreitol
-
required
Triton X-100
-
biphasic, optimal stimulation at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
acyl-carrier protein
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 10.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
not active below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
aggregates upon overexpression in vivo or concentration in vitro
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
x * 25000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 25000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D24N
low level of activity
D78N
no activity
D82N
no activity
H6Q
low level of activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
loss of activity after 15 min in the absence of SDS
90
-
stable in the presence of 1% SDS
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
90°C, 1% SDS, 10 min, 20% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding in purification step using Profoldin soluble protein folding column
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vagelos, P.R.; Larrabee, A.R.
Acyl carrier protein. IX. Acyl carrier protein hydrolase
J. Biol. Chem.
242
1776-1781
1967
Escherichia coli
Manually annotated by BRENDA team
Fischl, A.S.; Kennedy, E.P.
Isolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli
J. Bacteriol.
172
5445-5449
1990
Escherichia coli
Manually annotated by BRENDA team
Thomas, J.; Cronan, J.E.
The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization
J. Biol. Chem.
280
34675-34683
2005
Escherichia coli
Manually annotated by BRENDA team
Thomas, J.; Rigden, D.J.; Cronan, J.E.
Acyl carrier protein phosphodiesterase (AcpH) of Escherichia coli is a non-canonical member of the HD phosphatase/phosphodiesterase family
Biochemistry
46
129-136
2007
Escherichia coli (P21515), Escherichia coli
Manually annotated by BRENDA team
Thomas, J.; Cronan, J.E.
Antibacterial activity of N-pentylpantothenamide is due to inhibition of coenzyme A synthesis
Antimicrob. Agents Chemother.
54
1374-1377
2010
Escherichia coli
Manually annotated by BRENDA team