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Information on EC 2.3.1.31 - homoserine O-acetyltransferase and Organism(s) Haemophilus influenzae and UniProt Accession P45131

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This record set is specific for:
Haemophilus influenzae
UNIPROT: P45131 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
homoserine transacetylase, homoserine o-acetyltransferase, homoserine transsuccinylase, homoserine acetyltransferase, mshat, homoserine-o-transacetylase, cnhta, mtmetx, l-homoserine o-acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyltransferase, homoserine
-
-
-
-
homoserine acetyltransferase
-
-
-
-
homoserine transacetylase
homoserine-O-transacetylase
-
-
-
-
L-homoserine O-acetyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
show the reaction diagram
ping-pong reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-homoserine O-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-72-2
-
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-homoserine
CoA + O-acetyl-L-homoserine
show the reaction diagram
-
-
-
?
acetyl-CoA + 3-amino-1-propanol
?
show the reaction diagram
-
low activity
-
-
r
acetyl-CoA + 4-nitrophenyl acetate
?
show the reaction diagram
-
low activity
-
-
r
acetyl-CoA + D-homoserine
CoA + O-acetyl-D-homoserine
show the reaction diagram
-
-
-
-
r
acetyl-CoA + gamma-hydroxybutyric acid
?
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
show the reaction diagram
butyryl-CoA + L-homoserine
CoA + O-butyryl-L-homoserine
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + L-homoserine
CoA + O-crotonyl-L-homoserine
show the reaction diagram
-
low activity
-
-
r
glutaryl-CoA + L-homoserine
CoA + O-glutaryl-L-homoserine
show the reaction diagram
-
very low activity
-
-
r
propionyl-CoA + L-homoserine
CoA + O-propionyl-L-homoserine
show the reaction diagram
-
-
-
-
?
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
show the reaction diagram
-
very low activity
-
-
r
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-homoserine
CoA + O-acetyl-L-homoserine
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3S,4S)-4-heptyl-3-methyloxetan-2-one
-
-
4-nonyloxetan-2-one
-
-
ebelactone A
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
71
3-Amino-1-propanol
-
-
19
4-hydroxybutyric acid
-
-
1.4
4-nitrophenyl acetate
-
-
0.14
acetyl-CoA
-
-
0.21
butyryl-CoA
-
-
0.13
crotonyl-CoA
-
-
4.7
D-homoserine
-
-
0.28
glutaryl-CoA
-
-
0.13
L-homoserine
-
-
0.85
O-acetyl-L-homoserine
-
-
0.09
propionyl-CoA
-
-
0.36
succinyl-CoA
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
3-Amino-1-propanol
-
-
50
4-hydroxybutyric acid
-
-
7.8
4-nitrophenyl acetate
-
-
92
acetyl-CoA
-
-
27
butyryl-CoA
-
-
15
crotonyl-CoA
-
-
78
D-homoserine
-
-
92
L-homoserine
-
-
31
O-acetyl-L-homoserine
-
-
30
propionyl-CoA
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
(3S,4S)-4-heptyl-3-methyloxetan-2-one
-
pH 7.5, 37°C
0.084
4-nonyloxetan-2-one
-
pH 7.5, 37°C
0.203
ebelactone A
-
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme enables the survival of fungi and bacteria in methionine-poor environments such as blood serum, thus its inhibition can be deleterious for the organism
metabolism
-
first step in the biosynthesis of methionine from aspartic acid
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 35000-40000, SDS-PAGE and electrospray ionization-mass spectrometry
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure to a resolution of 1.65 A. The structure identifies this enzyme to be a member of the alpha/beta-hydrolase superfamily, possessing an additional lid domain with a novel fold
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S143A
-
mutant does not show any acetyltransferase activity. Incubation of mutant HTAH with ebelactone A and inhibitor does not generate an enzyme-inhibitor adduct
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from E. coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
met2 gene, expression in Escherichia coli BL21 (DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Born, T.L.; Franklin, M.; Blanchard, J.S.
Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase
Biochemistry
39
8556-8564
2000
Haemophilus influenzae
Manually annotated by BRENDA team
Mirza, I.A.; Nazi, I.; Korczynska, M.; Wright, G.D.; Berghuis, A.M.
Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases
Biochemistry
44
15768-15773
2005
Haemophilus influenzae (P45131), Haemophilus influenzae
Manually annotated by BRENDA team
De Pascale, G.; Nazi, I.; Harrison, P.H.; Wright, G.D.
beta-Lactone natural products and derivatives inactivate homoserine transacetylase, a target for antimicrobial agents
J. Antibiot.
64
483-487
2011
Haemophilus influenzae
Manually annotated by BRENDA team