Information on EC 2.3.1.31 - homoserine O-acetyltransferase

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

EC NUMBER
COMMENTARY hide
2.3.1.31
-
RECOMMENDED NAME
GeneOntology No.
homoserine O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Cysteine and methionine metabolism
-
-
L-homocysteine biosynthesis
-
-
Metabolic pathways
-
-
threonine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-homoserine O-acetyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-72-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
metA gene
-
-
Manually annotated by BRENDA team
anamorph: Fusarium graminearum, wild-type strain Z03643
-
-
Manually annotated by BRENDA team
metX gene
SwissProt
Manually annotated by BRENDA team
gene met2
-
-
Manually annotated by BRENDA team
gene dcsE; gene dcsE
UniProt
Manually annotated by BRENDA team
gene dcsE; gene dcsE
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
additional information
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 + 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
acetyl-CoA + gamma-hydroxybutyric acid
?
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-homoserine
CoA + O-acetyl-L-homoserine
show the reaction diagram
beta-hydroxybutyryl-CoA + L-homoserine
CoA + beta-hydroxybutyryl-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
isobutyryl-CoA + L-homoserine
CoA + O-isobutyryl-L-homoserine
show the reaction diagram
-
-
-
-
?
malonyl-CoA + L-homoserine
CoA + O-malonyl-L-homoserine
show the reaction diagram
-
-
-
-
?
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
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
succinyl-CoA + L-homoserine
CoA + O-succinyl-L-homoserine
show the reaction diagram
-
activity of mutant E111G
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3S,4S)-4-heptyl-3-methyloxetan-2-one
-
-
4-nonyloxetan-2-one
-
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6-carbamoyl-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
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competitive inhibitor of acetyl-CoA
acetylcarnitine
-
-
DL-Penicillamine
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3.3 mM, complete inhibition
ebelactone A
-
-
iodoacetamide
-
-
L-cysteine
-
weak
L-homocysteine
L-methionine
O-acetyl-L-homoserine
O-acetyl-L-serine
-
weak
O-phospho-L-homoserine
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weak
O-succinyl-L-homoserine
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weak
S-adenosyl-L-homocysteine
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weak
S-adenosyl-L-methionine
Zn2+
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reversible
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
71
3-Amino-1-propanol
-
-
19
4-hydroxybutyric acid
-
-
1.4
4-nitrophenyl acetate
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-
0.0116 - 3.07
acetyl-CoA
0.083
beta-hydroxybutyryl-CoA
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25C, pH 7.5
0.0441 - 0.21
butyryl-CoA
0.14 - 0.62
CoA
0.13
crotonyl-CoA
-
-
4.7 - 280
D-homoserine
0.18 - 0.28
glutaryl-CoA
0.068
isobutyryl-CoA
-
25C, pH 7.5
0.13 - 98
L-homoserine
0.017
malonyl-CoA
-
25C, pH 7.5
0.85
O-acetyl-L-homoserine
-
-
1.7
O-acetylhomoserine
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25C, pH 7.5
0.044 - 0.09
propionyl-CoA
0.051 - 0.36
succinyl-CoA
additional information
additional information
-
kcat/Km (substrate L-homoserine): 130000/Msec, (substrate acetyl-CoA): 878000/Msec
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
3-Amino-1-propanol
Haemophilus influenzae
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-
50
4-hydroxybutyric acid
Haemophilus influenzae
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-
7.8
4-nitrophenyl acetate
Haemophilus influenzae
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-
0.015 - 92
acetyl-CoA
0.12
beta-hydroxybutyryl-CoA
Thermotoga maritima
-
25C, pH 7.5
27 - 47.2
butyryl-CoA
1.9
CoA
Thermotoga maritima
-
25C, pH 7.5
15
crotonyl-CoA
Haemophilus influenzae
-
-
16 - 78
D-homoserine
0.25
glutaryl-CoA
Thermotoga maritima
-
25C, pH 7.5
0.19
isobutyryl-CoA
Thermotoga maritima
-
25C, pH 7.5
0.22 - 122
L-homoserine
0.12
malonyl-CoA
Thermotoga maritima
-
25C, pH 7.5
31
O-acetyl-L-homoserine
Haemophilus influenzae
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-
1.9
O-acetylhomoserine
Thermotoga maritima
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25C, pH 7.5
2.6 - 30
propionyl-CoA
0.19 - 0.803
succinyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0228 - 5.28
acetyl-CoA
29
0.0074 - 4.56
L-homoserine
345
2.94
succinyl-CoA
Bacillus cereus
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E111G, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25C
224
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
(3S,4S)-4-heptyl-3-methyloxetan-2-one
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pH 7.5, 37C
0.084
4-nonyloxetan-2-one
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pH 7.5, 37C
0.0136 - 0.0917
6-carbamoyl-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
0.203
ebelactone A
-
pH 7.5, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.156 - 0.287
6-carbamoyl-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0036
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-
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 7.5
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assay at
additional information
-
pI: 4.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 9
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more than half-maximal activity over this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
1 * 37000, SDS-PAGE
41000
-
amino acid sequence determination
73000
-
gel filtration
101000 - 104000
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sucrose density gradient centrifugation, gel filtration
additional information
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amino acid sequence comparison
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 35000-40000, SDS-PAGE and electrospray ionization-mass spectrometry
homodimer
monomer
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1 * 37000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with homoserine, hanging drop vapor diffusion, purified protein is added to 1.4 M (NH4)2SO4 and 0.1 M Tris, pH 8.0, soaked with 1.8 M (NH4)2SO4 and same buffer containing 15% glycerol, and 10 mM homoserine, crystals are flash frozen; x-ray crystal structure at 2.0 A of the Bacillus cereus metA protein in complex with homoserine is presented
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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
crystal structure of HTA from Leptospira interrogans is determined at 2.2 A resolution using selenomethionyl single-wavelength anomalous diffraction method. HTA is modular and consists of two structurally distinct domains: a core alpha/beta domain containing the catalytic site and a helical bundle called the lid domain. Structure fold belongs to alpha/beta hydrolase superfamily with the characteristic catalytic triad residues in the active site. The catalytic His and Ser are both present in two conformations, which may be involved in the catalytic mechanism for acetyl transfer
purified recombinant apoenzyme, hanging-drop vapor-diffusion method, mixing of 0.001 ml of 5 mg/ml protein solution with 0.001 ml of well solution, containing 0.7 M ammonium formate, 100 mM imidazole-HCl, pH 6.5, 20C, 5-7 days, X-ray diffraction structure determination and analysis at 2.45 A resolution
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purified recombinant wild-type and mutant G52A-P55G enzymes, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml of protein in 20 mM Tris-HCl, pH 7.6, 0.2 M NaCl, 5 mM dithiothreitol, and 1 mM EDTA, with 0.001 ml of precipitant solution containing 0.1 M Tris-HCl, pH 7.5, 25% w/v PEG 4000, and 0.2 M ammonium acetate, 3 weeks, structure modeling, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
most stable
486784
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
t1/2: 15 min
8
-
t1/2: 10 min
25
-
most rapid and irreversible inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
temperature inactivation readily reversible
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, t1/2: 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cells are centrifuged in 50 mM Tris, pH 8.0, sonicated, centrifuged, supernatant loaded to a Ni2+-nitrilotriacetic acid-agarose column, washed, and eluted, eland incubated with protease and dialyzed, reloaded onto a Ni2+-nitrilotriacetic acid-agarose column, dialyzed, loaded onto Superdex-200 size-exclusion fast protein liquid chromatography column with 25 mM HEPES-buffer, pH 7.5; using Ni-NTA-chromatography
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partial
partial, mutant strain 6
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recombinant from E. coli
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion excange chromatography, followed by gel electrophoresis, dialysis, and ultrafiltration
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recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, dialysis and ultrafiltration
using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amplification, expression in Escherichia coli BL21(DE3); expressed in Escherichia coli as a His-tagged fusion protein
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expressed in Escherichia coli as a His-tagged fusion protein
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expression in Escherichia coli
gene dcsE, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene met2, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)
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met2 gene, expression in Escherichia coli BL21 (DE3)
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met2-gene, expression in Escherichia coli DH1, DNA and amino acid sequence determination
metA gene, complementation of Escherichia coli metA deficient mutant, DNA sequence determination
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mutant enzymes expressed in Saccharomyces cerevisiae
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overexpression of metX in Escherichia coli BL21 (DE3), complementation of Escherichia coli metA deficient mutant, amino acid sequence determination
subcloning in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C142A
-
enzyme inactive; inactive enzyme
C142S
-
enzyme inactive; inactive enzyme
E111G
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mutant protein shows no detectable activity with acetyl-CoA but catalyzes an acyltransferase reaction using succinyl-CoA and homoserine (kcat (succinyl-CoA): 0.8/sec, Km (succinyl-CoA): 0.273 mM, Km (L-homoserine): 0.2 mM); no activity with acetyl-CoA, but with succinyl-CoA and homoserine, glutamic acid 111 (corresponding to Escherichia coli residue with function in succinyl-specificity of homoserine transsuccinylase) sterically occludes fitting of a succinyl-enzyme intermediate in the active site
E237A
-
compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased; decrease in catalytic activity
E237D
-
compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased; decrease in catalytic activity
E237Q
-
compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased; decrease in catalytic activity
E250A
-
13-14fold increase in homoserine Km value, homoserine binding is affected not acetyl-CoA binding; compared to wild-type: kcat and Km (acetyl-CoA) decreased, Km (L-homoserine) increased
H235A
-
enzyme inactive; inactive enzyme
H235N
-
enzyme inactive; inactive enzyme
H235Q
-
enzyme inactive; inactive enzyme
K163M
-
13-14fold increase in homoserine Km value, homoserine binding is affected not acetyl-CoA binding; compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
K47M
-
compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased; turnover number is reduced 14fold, Km value for acetyl-CoA is reduced 17fold, function in acetyl-CoA binding
K47R
-
compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased; Km value for acetyl-CoA is affected, function in acetyl-CoA binding
R249M
-
10fold reduction in kcat, 64fold higher Km for homoserine than wild-type, homoserine binding is affected not acetyl-CoA binding; compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
S192A
-
5fold increase in Km for homoserine, homoserine binding is affected not acetyl-CoA binding; compared to wild-type: kcat (acetyl-CoA) decreased, Km (L-homoserine) and (acetyl-CoA) increased
S143A
-
mutant does not show any acetyltransferase activity. Incubation of mutant HTAH with ebelactone A and inhibitor does not generate an enzyme-inhibitor adduct
D209N
-
kcat/Km for acetyl-CoA is 1.45fold lower than wild-type value, kcat/Km for L-homocysteine is 1.6fold higher than wild-type value
D374N
-
kcat/Km for acetyl-CoA is 1.6fold than wild-type value, kcat/Km for L-homocysteine is 1.6fold higher than wild-type value
D403N
-
inactive mutant enzyme
H432A
-
inactive mutant enzyme
S163A
-
inactive mutant enzyme
S163C
-
kcat/Km for acetyl-CoA is 16.7fold than wild-type value, kcat/Km for L-homocysteine is 33fold lower than wild-type value
G52A
site-directed mutagenesis, no activity with L-serine, but with L-homoserine, although the mutant is less active than the wild-type enzyme
G52A/P55G
site-directed mutagenesis, no activity with L-serine, but with L-homoserine, activity with L-homoserine is increased compared to the wild-type enzyme
P55G
site-directed mutagenesis, increased activity with L-serine and with L-homoserine compared to the wild-type enzyme
G52A
-
site-directed mutagenesis, no activity with L-serine, but with L-homoserine, although the mutant is less active than the wild-type enzyme
-
P55G
-
site-directed mutagenesis, increased activity with L-serine and with L-homoserine compared to the wild-type enzyme
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
using a mouse inhalation model of infection it is shown that MET2 is required for virulence, making fungal HTA a viable target for new antibiotic discovery
molecular biology
-
the HOA gene can be used as a selectable marker for transformation of Gibberella zeae
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