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Information on EC 2.3.1.30 - serine O-acetyltransferase and Organism(s) Haemophilus influenzae and UniProt Accession P43886

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.30 serine O-acetyltransferase
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This record set is specific for:
Haemophilus influenzae
UNIPROT: P43886 not found.
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Word Map
The taxonomic range for the selected organisms is: Haemophilus influenzae
The enzyme appears in selected viruses and cellular organisms
Synonyms
serine acetyltransferase, sat-1, satase, hisat, serat, serine transacetylase, serine o-acetyltransferase, ehsat1, atsat1, atoass, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
serine O-acetyltransferase
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acetyltransferase, serine
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-
-
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L-serine acetyltransferase
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-
-
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SATase
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-
-
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serine acetyltransferase
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-
-
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serine transacetylase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
show the reaction diagram
ordered kinetic mechanism with acetyl CoA bound prior to L-serine and O-acetyl-L-serine released prior to CoA. The rate-limiting step along the reaction pathway is the nucleophilic attack of the serine hydroxyl on the thioester of acetyl CoA. Product release contributes to rate-limitation at saturating concentrations of reactants. The reaction is catalyzed by an active site general base with a pK of 7, which accepts a proton from the serine hydroxyl as a tetrahedral intermediate is formed between the reactants, and donates it to the thiol of CoA as the intermediate collapses to give products
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-serine O-acetyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-16-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
show the reaction diagram
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
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
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
show the reaction diagram
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enzyme catalyzes the committed step in the de novo synthesis of L-cysteine. Serine acetyltransferase is regulated by feedback inhibition by the end product L-cysteine, which acts by binding to the serine site in the active site and inducing a conformational change that prevents reactant binding
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycine
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competitive versus L-serine, uncompetitive versus acetyl-CoA
L-cysteine
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dead-end inhibitor, competitive against botn substrates in both reaction directions
L-serine
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product inhibition is noncompetitive with respect to O-acetyl-L-serine and CoA
O-acetyl-L-serine
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product inhibition is noncompetitive against acetyl-CoA and uncompetitive against L-serine
S-methyl-L-cysteine
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competitive versus O-acetyl-L-serine and competitive versus CoA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.7
acetyl-CoA
0.6 - 160
L-serine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of Haemophilus influenzae O-acetylserine sulfhydrylase (EC 2.5.1.47) in complex with the C-terminal 10-residue peptide of serine acetyltransferase are prepared under silicon oil by using the sitting drop method
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X-ray crystallographic structure of the enzyme in binary complexes with cysteine and CoA and refined to resolutions of 1.85 and 2.0 A, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D139N
Km (mM): 0.12 (acetyl-CoA), 160 (L-serine)
H154N
Km (mM): 0.21 (acetyl-CoA), 0.6 (L-serine)
H154N/H189N
Km (mM): 0.24 (acetyl-CoA), 27 (L-serine)
H189N
Km (mM): 32 (L-serine)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, C.M.; Huang, B.; Roderick, S.L.; Cook, P.F.
Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae
Arch. Biochem. Biophys.
429
115-122
2004
Haemophilus influenzae
Manually annotated by BRENDA team
Huang, B.; Vetting, M.W.; Roderick, S.L.
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
J. Bacteriol.
187
3201-3205
2005
Haemophilus influenzae
Manually annotated by BRENDA team
Johnson, C.M.; Roderick, S.L.; Cook, P.F.
The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol
Arch. Biochem. Biophys.
433
85-95
2005
Haemophilus influenzae
Manually annotated by BRENDA team
Campanini, B.; Speroni, F.; Salsi, E.; Cook, P.F.; Roderick, S.L.; Huang, B.; Bettati, S.; Mozzarelli, A.
Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy
Protein Sci.
14
2115-2124
2005
Haemophilus influenzae
Manually annotated by BRENDA team
Guan, R.; Roderick, S.L.; Huang, B.; Cook, P.F.
Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae
Biochemistry
47
6322-6328
2008
Haemophilus influenzae (P43886), Haemophilus influenzae
Manually annotated by BRENDA team