Information on EC 6.3.5.4 - Asparagine synthase (glutamine-hydrolysing)

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

EC NUMBER
COMMENTARY hide
6.3.5.4
-
RECOMMENDED NAME
GeneOntology No.
Asparagine synthase (glutamine-hydrolysing)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid amide hydrolysis
-
-
carboxylic
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-asparagine biosynthesis I
-
-
aspartate and asparagine metabolism
-
-
Alanine, aspartate and glutamate metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
L-Aspartate:L-glutamine amido-ligase (AMP-forming)
The enzyme from Escherichia coli has two active sites [4] that are connected by an intramolecular ammonia tunnel [5,6]. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a beta-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine [6].
CAS REGISTRY NUMBER
COMMENTARY hide
37318-72-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 168, three glutamine-dependent AsnB-type asparagine snythetase genes: asnB, asnH and asnO, formerly yisO
-
-
Manually annotated by BRENDA team
strain 168, three glutamine-dependent AsnB-type asparagine snythetase genes: asnB, asnH and asnO, formerly yisO
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
; gene CaAS1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
the organism contains both enzymes EC 6.3.1.1. and EC 6.3.4.5. The gene asnA codes for NH4+-dependent Asn synthetases, EC 6.3.1.1, and the gene asnB codes for Gln-dependent Asn synthetase, EC 6.3.5.4
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
v. Little Marvel, dark-grown
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isoforms StAs1 and StAs2
-
-
Manually annotated by BRENDA team
strain 139
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
enzyme form TaSN1; enzyme form TaSN2
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
Asn is a major amino acid in maize and since AsnS is the primary means of Asn synthesis in plants it plays a very important role in nitrogen metabolism; Asn is a major amino acid in maize and since AsnS is the primary means of Asn synthesis in plants it plays a very important role in nitrogen metabolism; Asn is a major amino acid in maize and since AsnS is the primary means of Asn synthesis in plants it plays a very important role in nitrogen metabolism; Asn is a major amino acid in maize and since AsnS is the primary means of Asn synthesis in plants it plays a very important role in nitrogen metabolism
physiological function
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
ATP + cysteine sulfinic acid
AMP + diphosphate + cysteine sulfinic acid
show the reaction diagram
-
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
show the reaction diagram
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
show the reaction diagram
ATP + L-Asp + L-Gln + H2O
AMP + diphosphate + L-Asn + L-Glu
show the reaction diagram
-
-
-
-
?
ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
show the reaction diagram
ATP + L-Asp + NH3
AMP + diphosphate + Asn
show the reaction diagram
ATP + L-Asp + NH3
AMP + diphosphate + L-Asn
show the reaction diagram
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
show the reaction diagram
CTP + L-Asp + L-Gln
CMP + diphosphate + Asn + Glu
show the reaction diagram
-
weak activity
-
-
-
dATP + L-Asp + L-Gln
dAMP + diphosphate + Asn + Glu
show the reaction diagram
-
utilized at a similar rate as ATP
-
-
-
dATP + L-Asp + NH3
dAMP + diphosphate + Asn
show the reaction diagram
-
utilized at a similar rate as ATP
-
-
-
GTP + L-Asp + L-Gln
GMP + diphosphate + Asn + Glu
show the reaction diagram
L-Glutamic acid gamma-monohydroxamate + H2O
Hydroxylamine + Glu
show the reaction diagram
-
-
-
-
-
L-glutamine
L-glutamate + NH3
show the reaction diagram
UTP + L-Asp + L-Gln
UMP + diphosphate + Asn + Glu
show the reaction diagram
-
weak activity
-
-
-
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
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
show the reaction diagram
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
show the reaction diagram
-
light, carbon and nitrogen availability control asparagine synthesis in sunflower by regulating three aspargine synthetase coding genes. HAS2 expression requires light and is positively affected by sucrose. HAS1 and HAS1.1 expression is dependent on nitrogen availability, while HAS2 transcripts are still found in N-starved plants. High ammonium level induces all three asparagine synthetase genes and partially reverts sucrose repression of HAS1 and HAS1.1
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
show the reaction diagram
L-glutamine
L-glutamate + NH3
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
at 16.7 mM CaCl2 31% of the activation relative to MgCl2
CN-
-
stimulates Asn synthesis and Gln hydrolysis
Cu2+
-
0.02 mM, induces expression of the enzyme
F-
-
stimulates Asn synthesis and Gln hydrolysis
FeCl2
-
at 16.7 mM FeCl2 39% of the activation relative to MgCl2
Na+
-
150 mM, induces expression of the enzyme
NO3-
-
stimulates Asn synthesis and Gln hydrolysis
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methyl-4-(1-methylethyl)-7-oxabicyclo[2.2.1]heptane
-
trivial name 1,4-cineole, almost complete inhibition above 1 mM
2,3-dicarboxypyridine
-
-
2,4-Dicarboxypyridine
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-
2,5-Dicarboxypyridine
-
-
2,6-dicarboxypyridine
-
-
2-Amino-2-carboxy-L-ethanesulfonamide
-
-
2-Amino-4-arsonophenol hydrochloride
-
-
2-carboxypyridine
-
-
2-Hydroxyethyl-L-Gln
-
-
2-oxoglutarate
3,4-Dicarboxypyridine
-
-
3,5-Dicarboxypyridine
-
-
4-Carboxypyridine
-
-
5'-O-[p-(fluorosulfonyl)benzoyl]adenosine
5-Bromo-4-oxo-L-norvaline
-
-
5-Chloro-4-oxo-L-norvaline
5-Diazo-4-oxo-L-norvaline
-
-
6-diazo-5-oxo-L-norleucine
8-N3ATP
-
loss of NH4+-dependent Asn synthesis, but no effect on the glutaminase activity
Adenosine-5'-methylphosphonate
-
-
adenylated sulfoximine
-
0.005 mM, 65% inhibition, dead-end complex with AS-B
ADP
-
weak
Albizzine
alpha,beta-methylene ATP
-
-
alpha,beta-methylene-ATP
-
-
aminomalonic acid
ammonium maleamate
-
weak
AMP-PNP
-
competitive vs. ATP, noncompetitive vs. aspartate, uncompetitive vs. glutamine
Arg
-
-
asparagine
aspartic acid analogs
-
-
ATP
-
strong inhibition above 5 mM
azaserine
beta,gamma-methylene ATP
-
-
beta-asparaginyladenylate
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-
beta-Methyl-DL-Asn
-
-
beta-methylaspartate
Carbamoyl phosphate
-
-
cis-2-hydroxy-1,4-cineole
-
0.00003 mM, 50% inhibition
Cl-
-
inhibition of the ammonia-dependent reaction, competitive with respect to ammonia, with negative cooperativity. Stimulation of the Gln-dependent and glutaminase reaction
CMP
-
weak
Cu2+
-
-
D-Aspartic acid
-
weak
diphosphate
DL-alpha-Aminotricarballylic acid
-
weak
DL-homo-Gln
-
-
erythro-beta-Hydroxy-L-Asn
-
-
erythro-beta-hydroxy-L-Asp
-
-
erythro-beta-Methyl-L-Asp
-
-
gamma-Methylene-L-Gln
-
-
GDP
-
weak
glutamate
Gly-L-Asn
-
weak
GMP
-
weak
IMP
-
weak
iodoacetamide
-
-
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydroisoxazol-5-ylacetic acid
-
i.e. NSC-163501
L-1-Amino-4-oxo-5-(5'-adenosyl)phosphopentanoic acid
-
noncompetitive with respect to Gln and uncompetitive with respect to both ATP and Asp
-
L-2-Amino-4-oxo-5-chloropentanoic acid
-
-
L-2-Amino-4-oxo-5-hydroxypentanoic acid
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-
L-2-Amino-4-oxo-5-methylphosphonopentanoic acid
-
-
L-asparagine
L-beta-Aspartate ethyl ester
-
-
L-cysteinesulfinic acid
-
-
L-glutamate
competitive inhibition
L-Glutamate diamide
-
-
L-Glutamate-gamma-ethyl ester
-
-
L-glutamate-gamma-methyl ester
-
-
L-glutamic acid gamma-methyl ester
-
-
L-glutamic acid gamma-methylester
-
uncompetitive vs. ATP, competitive vs. glutamine
L-Homoserine beta-adenylate
-
in the presence of 30 mM MgCl2
L-Malic acid
-
weak
L-methionine sulfoxide
-
-
L-methionine-S-sulfoximine
-
-
Maleimide
-
-
meso-Diaminosuccinamate
-
-
Methyl gamma-Gln
-
-
Mucochloric acid
-
-
mupirocin
-
-
N-acetyl-L-Gln
-
-
N-alpha-Methyl-L-Asn
-
-
N-Benzyloxycarbonyl-L-Asn
-
weak
N-Benzyloxycarbonyl-L-aspartate
-
weak
N-Carbobenzoxy-DL-Gln
-
-
N-ethyl-L-Asn
-
-
N-Methyl-DL-aspartic acid
-
-
N-Methyl-L-Asn
-
-
nucleoside triphosphates
-
except ATP
O-acetylserine
-
-
oxaloacetate
-
20 mM, 40% inhibition
p-chloromercuribenzoate
-
-
phosmidosine
-
-
Phthalic acid
-
weak
pyrrolidine-2,3-dicarboxylic acid
-
weak inhibitor
pyruvate
-
20 mM, 12-15% inhibition
S-Carbamoylcysteine
S-methyl-L-cysteine
-
-
S-methyl-L-cysteine-(RS)-sulfoximine
-
weak
Sn2+
-
-
Sr2+
-
-
sulfhydryl reagents
-
-
sulfoximine adenylate
-
most potent inhibitor
threo-beta-Hydroxy-L-Asn
-
-
threo-beta-methyl-L-Asp
-
-
trans-2-hydroxy-1,4-cineole
-
0.01 mM, 50% inhibition
Trp
-
-
UMP
-
weak
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycerol
mannitol
-
300 mM, induces expression of the enzyme
Phytohemagglutinin
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53 - 55.7
Asp
0.38
aspartic acid
-
pH 8, reaction with glutamine, C-terminally tagged recombinant enzyme
0.013 - 1
ATP
0.16 - 5.24
Gln
11.5 - 17.1
hydroxylamine
0.13 - 1.2
L-Asp
0.1 - 2
L-aspartate
1.3
L-aspartic acid
-
pH 8, reaction with NH3, C-terminally tagged recombinant enzyme
0.04 - 9
L-Gln
0.09 - 0.26
L-glutamic acid gamma-monohydroxamate
0.09 - 1.9
L-glutamine
0.076
MgATP2-
-
-
0.75 - 9.9
NH3
2.1 - 120
NH4+
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52 - 1.37
Asp
0.43 - 5.8
ATP
0.4 - 1.31
Gln
1.7 - 5.8
glutamine
1.03 - 1.17
hydroxylamine
0.3 - 0.75
L-Asp
5.8
L-asparagine
Vibrio cholerae
-
-
1.05 - 2.94
L-aspartate
1.3 - 1.7
L-aspartic acid
0.05 - 10.02
L-Gln
0.1 - 0.15
L-glutamic acid gamma-monohydroxamate
0.8 - 6.08
L-glutamine
1.8
NH3
Homo sapiens
-
pH 8, C-terminally tagged recombinant enzyme
0.59 - 0.65
NH4+
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.7 - 39.2
ATP
4
0.63 - 3.45
L-Asp
294
0.45 - 9.1
L-Gln
337
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1 - 3.7
alpha,beta-methylene-ATP
2.5
AMP
-
-
0.91
AMP-PNP
-
-
0.023
Asn
-
Kis, versus Gln
0.25
asparagine
pH 7.6, 22C
18
beta-methylaspartate
-
-
0.021 - 0.85
diphosphate
150
Glu
-
-
0.3
glutamate
pH 7.6, 22C
0.25
L-asparagine
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
1.1 - 7.2
L-cysteine sulfinic acid
0.3
L-glutamate
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
6.5 - 29
L-glutamic acid gamma-methyl ester
6.6
L-glutamic acid gamma-methylester
-
-
0.000285
sulfoximine adenylate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1 - 1.5
asparagine
1.2 - 1.3
glutamate
1.1 - 1.5
L-asparagine
1.2 - 1.3
L-glutamate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.096
-
-
0.17
-
-
0.193
-
-
0.395
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
Gln-dependent activity
6.5 - 8
-
-
6.6 - 8
-
-
7.4 - 7.6
-
Gln-dependent activity
7.5 - 8
-
-
7.6 - 8.2
-
-
7.6
assay at; assay at; assay at; assay at
7.8 - 8.5
-
broad optimum
7.8 - 8.2
-
-
7.9 - 8.3
-
-
8.2
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
minor variation of activity in this pH range
6.7 - 8.8
-
minor variation of activity in this pH range
6.9 - 8.3
-
80% of maximal activity at pH 6.9 and 8.3
7 - 9
-
pH 7.0: about 45% of maximal activity, pH 9.0: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.92
HvAS2, theoretical pI
6.14
HvAS1, theoretical pI
6.3 - 6.8
sequence calculation
6.4
-
deduced from amino acid sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
-
SDS-PAGE
65500
SDS-PAGE
70000
-
gel filtration
105000
-
gel filtration
110000 - 120000
-
HPLC gel filtration
110000
-
gel filtration
160000
-
substrate-free enzyme, gel filtration
230000
-
gel filtration
320000
-
in presence of MgCl2 and ATP association to a dimer, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 52500, possibly the enzyme population is heterogeneous with slight differences in subunit composition, SDS-PAGE after treatment with dimethyl suberimidate
tetramer
-
4 * 57000, denaturing PAGE
additional information
-
dimerization of the 160000 MW enzyme is induced by MgCl2 and ATP
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AS-B is dialyzed against 20 mM Bis-Tris, pH 6.5, 150 mM NaCl, 0.5 mM EDTA, and 2 mM dithiothreitol, crystals are grown by hanging drop vapor diffusion at 4C, AS-B solution is adjusted to 6.5 mg/ml and contains 10 mM MgCl2, 5 mM glutamine, and 10 mM AMP, 0.01 ml of protein solution are mixed with 0.01 ml precipitant solution containing 14% polyethylene glycol 8000 and 50 mM HEPES, pH 7.0, these droplets are suspended against wells containing 15% polyethylene glycol 8000 and 50 mM HEPES, pH 7.0, crystals diffract to 2.0 A
-
X-ray crystal structure of AS-B complexed with glutamine and AMP
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
most stable around pH 8 at 4C
1688
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
half-life: 90 s
45
-
5 min, unstable
56
-
half-life: 30 s
additional information
-
a combination of L-Asp, ATP, and Mg2+ protects against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is markedly decreased by freezing for 7 days at -87C in the presence of 1 mM dithiothreitol. Protection by 10 mM dithiothreitol
-
ATP protects from inactivation by UV irradiation in the presence of 8-N3ATP
-
enzyme requires protection by high levels of thiols, glycerol and substrates also stabilize
-
glycerol and 2-mercaptoethanol are essential for enzyme stability during purification at 4C
-
unstable enzyme, 20-25% v/v glycerol and 65-70 mM 2-mercaptoethanol stabilize during storage at low temperatures
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SDS
proteins are always extracted in buffer with 2% SDS, otherwise a high degree of degradation is detected
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, inactivated after 3 months, reactivation by addition of dithiothreitol
-
-25C, 60% loss of activity after 3 months
-
-25C, semicrude extract, 9-10 days, 50% loss of activity
-
-80C, recombinant C-terminally tagged enzyme is stable on prolonged storage
-
-80C, semicrude extract, over 3 weeks, 30% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
development of a method to refold recombinant AsnS from inclusion bodies; refolded, solubilized recombinant His-tagged isozyme AsnS1 by nickel affinity chromatography; refolded, solubilized recombinant His-tagged isozyme AsnS2 by nickel affinity chromatography, recombinant nontagged isozyme ZmAsnS2 from Escherichia coli by anion exchange chromatography; refolded, solubilized recombinant His-tagged isozyme AsnS4 by nickel affinity chromatography; refolded, solubilized recombinant His-tagged isozyme by nickel affinity chromatography
immunoaffinity purification
-
one-step immunoaffinity purification
-
partial
recombinant
-
recombinant fusion protein consisting of the 42 kDa N-terminal region of AS and a 17 kDa tagged-region from pET32a(+) expression plasmid
-
recombinant protein
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a fusion protein consisting of the 42 kDa N-terminal region of AS and a 17 kDa tagged-region from pET32a(+) expression plasmid, expression in Escherichia coli
-
and overexpression
-
C-terminally tagged enzyme, baculovirus-based expression system, the recombinant enzyme is correctly processed, exhibits high activity and is stable on prolonged storage at -80C
-
cDNA, from cell culture SB-P, sequencing
-
cloned into a 2 m plasmid, pBS24.1GAS, suitable for replication in a Saccharomyces cerevisiae ciro strain AB116
-
cloned into a temperature-sensitive low copy plasmid, pOU71
-
cloning and specificity of the amino acid-dependent contol of its mRNA content
-
cloning of cDNA
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; gene asnS2, expression of nontagged isozyme ZmAsnS2 in Escherichia coli, expression of C-terminally His-tagged isozyme AsnS2 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies although small amounts of ZmAsnS2 are recovered in the soluble fraction; gene asnS3, expression of C-terminally His-tagged isozyme AsnS3 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies; gene asnS4, expression of C-terminally His-tagged isozyme AsnS4 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies; gene asnS, expression of C-terminally His-tagged isozyme AsnS1 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies
expression of AS-GFP fusion protein in MOLT-4 cells
-