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

EC NUMBER
COMMENTARY
6.3.5.4
-
RECOMMENDED NAME
GeneOntology No.
Asparagine synthase (glutamine-hydrolysing)
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acid amide hydrolysis
-
-
carboxylic
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
asparagine biosynthesis I
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AS
Q84LA5
-
AS-B
-
-
-
-
AS1
Q6HA26
-
ASNase
-
-
AsnB
-
-
-
-
ASNS
P08243
-
AsnS1
B4FFJ0
-
AsnS2
B5U8J7
-
AsnS3
B5U8J8
-
AsnS4
B5U8J9
-
asparagine amidotransferase
A9XS73
-
Asparagine synthetase
-
-
Asparagine synthetase
-
-
Asparagine synthetase
P08243
-
Asparagine synthetase
-
-
Asparagine synthetase
-
-
Asparagine synthetase
A9XS73
-
Asparagine synthetase
Q6HA26
-
Asparagine synthetase (glutamine hydrolyzing)
-
-
-
-
Asparagine synthetase (glutamine)
-
-
-
-
Asparagine synthetase (glutamine-hydrolysing)
-
-
-
-
asparagine synthetase 2
-
-
Asparagine synthetase B
-
-
-
-
Asparagine synthetase B
-
-
asparagine synthetase, glutamine-dependent
-
-
glutamine-dependent amidotransferase
-
-
Glutamine-dependent asparagine synthetase
-
-
-
-
HvAS1 protein
Q93XP9
Hordeum vulgare
HvAS2 protein
Q84LA5
Hordeum vulgare
L-asparaginase
-
-
L-Asparagine synthetase
-
-
-
-
PVAS1 protein
Q9SM55
Phaseolus vulgaris
Ste10
Q8KN11
-
Synthetase, Asn (glutamine)
-
-
-
-
TS11 cell cycle control protein
-
-
-
-
type -II asparagine synthetase
-
-
type I asparagine synthetase
Q9SM55
-
type II asparagine synthetase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37318-72-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 168, three glutamine-dependent AsnB-type asparagine snythetase genes: asnB, asnH and asnO, formerly yisO
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168, three glutamine-dependent AsnB-type asparagine snythetase genes: asnB, asnH and asnO, formerly yisO
-
-
Manually annotated by BRENDA team
ox
-
-
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
Asn synthetase B
-
-
Manually annotated by BRENDA team
Asn synthetase B; wild-type enzyme and mutant N74S
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes C1A, C1S, H29A , H80A, D33N, D33E, and A104H
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes C99A, C168A, C386A, C423A, C436A, C514A, C523A
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes R30A, R30K, N74A, N74Q, N79A
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes, E317A, E317Q, T318A, Y319A, Y319F, D320A, V321A, T322A, T322S, T322V, T322Y, T323A, T323I, T323L, T323S, T323V, R325A, R325K, T328S
-
-
Manually annotated by BRENDA team
wild-type and mutant N74A
-
-
Manually annotated by BRENDA team
cv. Corsoy
-
-
Manually annotated by BRENDA team
isoform SAS3
UniProt
Manually annotated by BRENDA team
isoforms SAS1 and SAS2
-
-
Manually annotated by BRENDA team
isoforms SAS1, SAS2
-
-
Manually annotated by BRENDA team
Merr. v. DP3588
-
-
Manually annotated by BRENDA team
cultivar HA-89
-
-
Manually annotated by BRENDA team
HAS1.1
SwissProt
Manually annotated by BRENDA team
patients with acute lymphoblastic leukemia
SwissProt
Manually annotated by BRENDA team
cv. Alexis, HvAS1, two AS genes: HvAS1 and HvAS2
SwissProt
Manually annotated by BRENDA team
cv. Alexis, HvAS2, two AS genes: HvAS1 and HvAS2
SwissProt
Manually annotated by BRENDA team
v. Victoria
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Sasanishiki
-
-
Manually annotated by BRENDA team
cv. Great Northern
SwissProt
Manually annotated by BRENDA team
cv. Negro Jamapa, gene NAS2
UniProt
Manually annotated by BRENDA team
v. Little Marvel, dark-grown
-
-
Manually annotated by BRENDA team
2 distinct Gln-dependent Asn synthetases
-
-
Manually annotated by BRENDA team
wild-type and auxotroph mutants
-
-
Manually annotated by BRENDA team
isoforms StAs1 and StAs2
-
-
Manually annotated by BRENDA team
strain 139
UniProt
Manually annotated by BRENDA team
enzyme form TaSN1; enzyme form TaSN2
-
-
Manually annotated by BRENDA team
isoform AsnS1
-
Manually annotated by BRENDA team
isoform AsnS2
-
Manually annotated by BRENDA team
isoform AsnS3
-
Manually annotated by BRENDA team
isoform AsnS4
-
Manually annotated by BRENDA team
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8.7
-
ATP
-
wild-type, ammonia-dependent activity, pH 8.0, 37C; wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37C
22040
9
-
ATP
-
wild-type, glutamine-dependent activity, pH 8.0, 37C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37C
22040
14.3
-
ATP
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37C; mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37C
22040
39.2
-
ATP
-
mutant E348D, glutamine-dependent activity, pH 8.0, 37C; mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37C
22040
0.63
-
L-Asp
-
wild-type, ammonia-dependent activity, pH 8.0, 37C; wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37C
12107
1.2
-
L-Asp
-
wild-type, glutamine-dependent activity, pH 8.0, 37C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37C
12107
1.3
-
L-Asp
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37C; mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37C
12107
3.4
-
L-Asp
-
mutant E348D, glutamine-dependent activity, pH 8.0, 37C
12107
3.45
-
L-Asp
-
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37C
12107
0.45
-
L-Gln
-
mutant E348Q, glutaminase activity, pH 8.0, 37C, ATP absent
12204
1.1
-
L-Gln
-
mutant E348A, glutaminase activity, pH 8.0, 37C, ATP absent
12204
1.14
-
L-Gln
-
mutant E348Q, glutaminase activity, pH 8.0, 37C, 5 mM ATP present
12204
1.19
-
L-Gln
-
wild-type, glutaminase activity, pH 8.0, 37C, ATP absent
12204
1.51
-
L-Gln
-
mutant E348D, glutaminase activity, pH 8.0, 37C, ATP absent
12204
1.66
-
L-Gln
-
mutant E348A, glutaminase activity, pH 8.0, 37C, 5 mM ATP present
12204
3.88
-
L-Gln
-
wild-type, glutaminase activity, pH 8.0, 37C, 5 mM ATP present
12204
9.1
-
L-Gln
-
mutant E348D, glutaminase activity, pH 8.0, 37C, 5 mM ATP present
12204
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.1
-
asparagine
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, 22C
1.3
-
asparagine
-
pH 7.6, 22C
1.3
-
asparagine
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, 22C
1.4
-
asparagine
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, 22C
1.5
-
asparagine
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, 22C
1.2
-
glutamate
-
pH 7.6, 22C
1.2
-
glutamate
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, 22C
1.3
-
glutamate
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, 22C; pH 7.6, 22C; pH 7.6, 22C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.92
-
-, Q84LA5, Q93XP9
HvAS2, theoretical pI
6.14
-
-, Q84LA5, Q93XP9
HvAS1, theoretical pI
6.3
6.8
Q9SM55
sequence calculation
6.4
-
-
deduced from amino acid sequence
6.5
-
B3KYI2
calculated
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SDS
Q6HA26
proteins are always extracted in buffer with 2% SDS, otherwise a high degree of degradation is detected
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
infection with Xanthomonas campestris pv. vesicatoria induces early and strong CaAS1 expression in leaves. Significant induction of CaAS1 expression occurs in pepper leaves following treatment with salicylic acid, methyl jasmonate or wounding
-