Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.5.4 - asparagine synthase (glutamine-hydrolysing) and Organism(s) Homo sapiens and UniProt Accession P08243

for references in articles please use BRENDA:EC6.3.5.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme from Escherichia coli has two active sites 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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P08243
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-asparaginase, asnase, asparagine synthetase b, glutamine-dependent asparagine synthetase, pvas2, taasn2, osas1, taasn1, glutamine-dependent amidotransferase, ste10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Asparagine synthetase
-
AS-B
-
-
-
-
ASNase
-
-
AsnB
-
-
-
-
Asparagine synthetase
-
-
Asparagine synthetase (glutamine hydrolyzing)
-
-
-
-
Asparagine synthetase (glutamine)
-
-
-
-
Asparagine synthetase (glutamine-hydrolysing)
-
-
-
-
Asparagine synthetase B
-
-
-
-
asparagine synthetase, glutamine-dependent
-
-
Glutamine-dependent asparagine synthetase
-
-
-
-
L-Asparagine synthetase
-
-
-
-
Synthetase, Asn (glutamine)
-
-
-
-
TS11 cell cycle control protein
-
-
-
-
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 mechanism, structure-function relationship
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
show the reaction diagram
ATP + L-Asp + NH3
AMP + diphosphate + 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
-
-
-
-
?
additional information
?
-
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
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 + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
show the reaction diagram
-
the basic region leucine zipper protein ATF5, a transcriptional activator, stimulates asparagine promoter/reporter gene transcription via the nutrient-sensing response unit
-
-
?
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
-
-
-
-
?
additional information
?
-
-
upregulation of asparagine synthetase fails to avert cell cycle arrest induced by L-asparaginase in TEL/AML1-positive leukaemic cells
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-diazo-5-oxo-L-norleucine
-
loss of Gln-dependent reactions, but no effect on ATP binding as measured during amminoa-dependent Asn synthesis
8-N3ATP
-
loss of NH4+-dependent Asn synthesis, but no effect on the glutaminase activity
beta-asparaginyladenylate
-
-
Gln
-
0.4-2.0 mM, inhibits the ammonia-dependent production of Asn
mupirocin
-
-
phosmidosine
-
-
sulfoximine adenylate
-
most potent inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phytohemagglutinin
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
aspartic acid
-
pH 8, reaction with glutamine, C-terminally tagged recombinant enzyme
0.08 - 0.11
ATP
1.3
L-aspartic acid
-
pH 8, reaction with NH3, C-terminally tagged recombinant enzyme
1.9
L-glutamine
-
pH 8, C-terminally tagged recombinant enzyme
1.7
NH3
-
pH 8, C-terminally tagged recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 1.7
ATP
1.7
glutamine
-
pH 8, C-terminally tagged recombinant enzyme
1.3 - 1.7
L-aspartic acid
1.8
NH3
-
pH 8, C-terminally tagged recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000285
sulfoximine adenylate
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
high expression in T-lineage and low expression in B-lineage
Manually annotated by BRENDA team
-
higher expression than in lymphoblastic leukemia cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
asparagine synthetase deficiency, ASD, is a neurological disorder having severe impacts on psychomotor development and mortality at an early age. Children with mutations in the ASNS gene exhibit developmental delays, intellectual disability, microcephaly, intractable seizures, and progressive brain atrophy. Mutations in the ASNS gene have been clinically associated with asparagine synthetase deficiency (ASD), phenotype. Neurologic disorder associated with asparagine synthetase deficiency (ASD). The transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription. Role of ATF4 in tumor cell survival and proliferation, ATF4 knockdown causes reduced survival in HT-1080 fibrosarcoma and DLD-1 colorectal adenocarcinoma cells in the absence of nonessential amino acids. Reduced proliferative capacity and increased apoptosis correlate with lower ASNS expression in the ATF4-deficient cells. Supplementation of the tumor cells with asparagine, but not other amino acids, leads to increased cell survival. Role of ASNS activity in modulating tumor growth
physiological function
asparagine synthetase (ASNS) catalyzes the synthesis of asparagine and glutamate from aspartate and glutamine in an ATP-dependent amidotransferase reaction. Elevated ASNS protein expression is associated with resistance to asparaginase therapy in childhood acute lymphoblastic leukemia. Regulation of ASNS expression, overview. transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription. Asparagine depletion activates the amino acid response, AAR, whereas endoplasmic reticulum stress activates the unfolded protein response, UPR
malfunction
-
knockdown of asparagine synthetase (ASNS) leads to cell death even in the presence of glutamine, which can be reversed by addition of exogenous asparagine. Asparagine plays a critical role in regulating cellular adaptation to glutamine depletion. ASNS knockdown leads to profound apoptosis even in the presence of glutamine. Addition of extracellular asparagine completely restored cell survival and proliferation. Clinically, the expression of ASNS correlates with the progression of disease and poor prognosis of glioma and neuroblastoma patients. In neuroblastoma with unfavourable prognosis, ASNS expression is significantly higher. Asparagine-induced suppression of apoptosis: asparagine addition to glutamine-deprived cells alters the transcriptional response, suppressing the induction of the reported UPR effectors CHOP and XBP1 while maintaining the transcriptional induction of adaptive components of the UPR-response such as ASNS and HERPUD1. At the protein level, exogenous addition of asparagine suppresses CHOP induction without altering ATF4 accumulation or upstream eIF2alpha phosphorylation
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASNS_HUMAN
561
0
64370
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme contains two functional domains, the N-terminal domain (residues 1-208) consists of a two-layer, antiparallel beta-sheet core surrounded by four alpha-helices, this domain harbors the glutamine-binding pocket, consisting of residues Arg49, Asn75, Glu77, and Asp97. The C-terminal domain (residues 209-561) is composed primarily of alpha-helices, but also encompasses a five-stranded, parallel beta-sheet that contains the ATP-binding site: residues Leu256, Val288, Asp295, Ser363, Gly364, Glu365, and Asp401
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A380S
naturally occuring mutation, homozygous mutation, mutation of a polar residue in the hydrophobic region
A6E
naturally occuring mutation, compound heterozygous, mutation of a charged amino acid in hydrophobic region, causing steric clash with Phe8
F362V
naturally occuring mutation, homozygous mutation, causes a decrease in van der Waals interactions
G289A
naturally occuring mutation, compound heterozygous, mutation proximal to the ATP-binding site, causing steric hindrance with Ser293
L145S
naturally occuring mutation, compound heterozygous, mutation of a polar side chain in hydrophobic region
L247W
naturally occuring mutation, causes a decrease in van der Waals interactions
R340H
naturally occuring mutation, homozygous mutation, causes a loss of hydrogen bonds, and a steric clash with Phe482
R49Q
naturally occuring mutation, homozygous mutation of the glutamine-binding site, causes loss of hydrogen bonding
R550C
S480F
naturally occuring mutation, compound heterozygous, mutation of a nonpolar residue on protein surface that may decrease solubility
T337I
naturally occuring mutation, Proximal to ATP-binding site, causes a hydrophobic patch on protein that may decrease solubility
V489D
naturally occuring mutation, compound heterozygous, inserts a charged amino acid in hydrophobic region
Y398C
naturally occuring mutation, homozygous mutation, causes a decrease in van der Waals interactions, solvent-accessible thiol group
C1A
-
altering Cys-1 to either Ala or Ser eliminated the Gln-dependent activity, while only minimally affecting the kinetic properties of the NH4+-dependent reaction
C1S
-
altering Cys-1 to either Ala or Ser eliminated the Gln-dependent activity, while only minimally affecting the kinetic properties of the NH4+-dependent reaction
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP protects from inactivation by UV irradiation in the presence of 8-N3ATP
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, recombinant C-terminally tagged enzyme is stable on prolonged storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
one-step immunoaffinity purification
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ASNS, a single copy gene located on chromosome 7
C-terminally tagged enzyme, baculovirus-based expression system, the recombinant enzyme is correctly processed, exhibits high activity and is stable on prolonged storage at -80°C
-
cloned into a 2 mü plasmid, pBS24.1GAS, suitable for replication in a Saccharomyces cerevisiae ciro strain AB116
-
expression of AS-GFP fusion protein in MOLT-4 cells
-
expression of several mutant enymes in Saccharomyces cerevisiae
-
mutant enzyme in which the N-terminal Cys is replaced by Ala is expressed in Saccharomyces
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ASNS activity is highly responsive to cellular stress, primarily by increased transcription from the single gene located on chromosome 7. The transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription
human enzyme activity is highly regulated in response to cell stress, primarily by increased transcription from a single gene located on chromosome 7. Protein limitation or an imbalanced dietary amino acid composition activate the ASNS gene through the amino acid response, a process that is replicated in cell culture through limitation for any single essential amino acid. Endoplasmic reticulum stress also increases ASNS transcription through the PERK-eIF2-ATF4 arm of the unfolded protein response. Both the amino acid response and unfolded protein response lead to increased synthesis of ATF4, which binds to the C/EBP-ATF response element and induces ASNS transcription
-
transcription factor ATF4 induces asparagine synthetase which results in glutamine-dependent asparagine synthesis from aspartate, in turn asparagine accumulation then suppresses GCN2 and reduces ATF4
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
mass spectrometry-based procedure for the direct quantification of asparagine synthetase protein concentration in complex sample mixtures. Assay is able to distinguish samples from transformed cell lines that express the enzyme over a wide dynamic range of concentration. The method directly detects asparagine synthetase protein, use in blast samples from patients with acute lymphoblastic leukemia
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sheng, S.; Moraga, D.A.; van Heeke, G.; Schuster, S.M.
High-level expression of human asparagine synthetase and production of monoclonal antibodies for enzyme purification
Protein Expr. Purif.
3
337-346
1992
Homo sapiens
Manually annotated by BRENDA team
Van Heeke, G.; Schuster, S.M.
The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity
J. Biol. Chem.
264
19475-19477
1989
Homo sapiens
Manually annotated by BRENDA team
Sheng, S.; Moraga-Amador, D.A.; van Heeke, G.; Allison, R.D.; Richards, N.G.J.; Schuster, S.M.
Glutamine inhibits the ammonia-dependent activities of two Cys-1 mutants of human asparagine synthetase through the formation of an abortive complex
J. Biol. Chem.
268
16771-16780
1993
Homo sapiens
Manually annotated by BRENDA team
Campaigne Larsen, M.; Schuster, S.M.
The topology of the glutamine and ATP binding sites of human asparagine synthetase
Arch. Biochem. Biophys.
299
15-22
1992
Homo sapiens
Manually annotated by BRENDA team
Milman, H.A.; Cooney, D.A.
The distribution of L-asparagine synthetase in the principal organs of several mammalian and avian species
Biochem. J.
142
27-35
1974
Bos taurus, Canis lupus familiaris, Cavia porcellus, Gallus gallus, Oryctolagus cuniculus, Felis catus, Ovis aries, Homo sapiens, Lupinus albus, Meleagris gallopavo, Platyrrhini, Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Aslanian, A.M.; Fletcher, B.S.; Kilberg, M.S.
Asparagine synthetase expression alone is sufficient to induce l-asparaginase resistance in MOLT-4 human leukaemia cells
Biochem. J.
357
321-328
2001
Homo sapiens
Manually annotated by BRENDA team
Dubbers, A.; Wurthwein, G.; Muller, H.J.; Schulze-Westhoff, P.; Winkelhorst, M.; Kurzknabe, E.; Lanvers, C.; Pieters, R.; Kaspers, G.J.L.; Creutzic, U.; Ritter, J.; Boos, J.
Asparagine synthetase activity in paediatric acute leukaemias: AML-M5 subtype shows lowest activity
Br. J. Haematol.
109
427-429
2000
Homo sapiens
Manually annotated by BRENDA team
Ciustea, M.; Gutierrez, J.A.; Abbatiello, S.E.; Eyler, J.R.; Richards, N.G.
Efficient expression, purification, and characterization of C-terminally tagged, recombinant human asparagine synthetase
Arch. Biochem. Biophys.
440
18-27
2005
Homo sapiens
Manually annotated by BRENDA team
Al Sarraj, J.; Vinson, C.; Thiel, G.
Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP
Biol. Chem.
386
873-879
2005
Homo sapiens
Manually annotated by BRENDA team
Stams, W.A.; den Boer, M.L.; Holleman, A.; Appel, I.M.; Beverloo, H.B.; van Wering, E.R.; Janka-Schaub, G.E.; Evans, W.E.; Pieters, R.
Asparagine synthetase expression is linked with L-asparaginase resistance in TEL-AML1-negative but not TEL-AML1-positive pediatric acute lymphoblastic leukemia
Blood
105
4223-4225
2005
Homo sapiens
Manually annotated by BRENDA team
Krejci, O.; Starkova, J.; Otova, B.; Madzo, J.; Kalinova, M.; Hrusak, O.; Trka, J.
Upregulation of asparagine synthetase fails to avert cell cycle arrest induced by L-asparaginase in TEL/AML1-positive leukaemic cells
Leukemia
18
434-441
2004
Homo sapiens
Manually annotated by BRENDA team
Richards, N.G.; Kilberg, M.S.
Asparagine synthetase chemotherapy
Annu. Rev. Biochem.
75
629-654
2006
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Leslie, M.; Case, M.C.; Hall, A.G.; Coulthard, S.A.
Expression levels of asparagine synthetase in blasts from children and adults with acute lymphoblastic leukaemia
Br. J. Haematol.
132
740-742
2006
Homo sapiens
Manually annotated by BRENDA team
Cui, H.; Darmanin, S.; Natsuisaka, M.; Kondo, T.; Asaka, M.; Shindoh, M.; Higashino, F.; Hamuro, J.; Okada, F.; Kobayashi, M.; Nakagawa, K.; Koide, H.; Kobayashi, M.
Enhanced expression of asparagine synthetase under glucose-deprived conditions protects pancreatic cancer cells from apoptosis induced by glucose deprivation and cisplatin
Cancer Res.
67
3345-3355
2007
Homo sapiens (P08243)
Manually annotated by BRENDA team
Iwamoto, S.; Mihara, K.; Downing, J.R.; Pui, C.H.; Campana, D.
Mesenchymal cells regulate the response of acute lymphoblastic leukemia cells to asparaginase
J. Clin. Invest.
117
1049-1057
2007
Homo sapiens
Manually annotated by BRENDA team
Chen, H.; Kilberg, M.S.
Alignment of the transcription start site coincides with increased transcriptional activity from the human asparagine synthetase gene following amino acid deprivation of HepG2 cells
J. Nutr.
136
2463-2467
2006
Homo sapiens
Manually annotated by BRENDA team
Fujita, Y.; Ito, M.; Nozawa, Y.; Yoneda, M.; Oshida, Y.; Tanaka, M.
CHOP (C/EBP homologous protein) and ASNS (asparagine synthetase) induction in cybrid cells harboring MELAS and NARP mitochondrial DNA mutations
Mitochondrion
7
80-88
2007
Homo sapiens
Manually annotated by BRENDA team
Lorenzi, P.L.; Reinhold, W.C.; Rudelius, M.; Gunsior, M.; Shankavaram, U.; Bussey, K.J.; Scherf, U.; Eichler, G.S.; Martin, S.E.; Chin, K.; Gray, J.W.; Kohn, E.C.; Horak, I.D.; Von Hoff, D.D.; Raffeld, M.; Goldsmith, P.K.; Caplen, N.J.; Weinstein, J.N.
Asparagine synthetase as a causal, predictive biomarker for L-asparaginase activity in ovarian cancer cells
Mol. Cancer Ther.
5
2613-2623
2006
Homo sapiens
Manually annotated by BRENDA team
Su, N.; Pan, Y.X.; Zhou, M.; Harvey, R.C.; Hunger, S.P.; Kilberg, M.S.
Correlation between asparaginase sensitivity and asparagine synthetase protein content, but not mRNA, in acute lymphoblastic leukemia cell lines
Pediatr. Blood Cancer
50
274-279
2008
Homo sapiens
Manually annotated by BRENDA team
Abbatiello, S.E.; Pan, Y.X.; Zhou, M.; Wayne, A.S.; Veenstra, T.D.; Hunger, S.P.; Kilberg, M.S.; Eyler, J.R.; Richards, N.G.; Conrads, T.P.
Mass spectrometric quantification of asparagine synthetase in circulating leukemia cells from acute lymphoblastic leukemia patients
J. Proteomics
71
61-70
2008
Homo sapiens (P08243)
Manually annotated by BRENDA team
Lorenzi, P.L.; Llamas, J.; Gunsior, M.; Ozbun, L.; Reinhold, W.C.; Varma, S.; Ji, H.; Kim, H.; Hutchinson, A.A.; Kohn, E.C.; Goldsmith, P.K.; Birrer, M.J.; Weinstein, J.N.
Asparagine synthetase is a predictive biomarker of L-asparaginase activity in ovarian cancer cell lines
Mol. Cancer Ther.
7
3123-3128
2008
Homo sapiens (P08243), Homo sapiens
Manually annotated by BRENDA team
Balasubramanian, M.N.; Butterworth, E.A.; Kilberg, M.S.
Asparagine synthetase: regulation by cell stress and involvement in tumor biology
Am. J. Physiol. Endocrinol. Metab.
304
E789-E799
2013
Homo sapiens
Manually annotated by BRENDA team
Lomelino, C.L.; Andring, J.T.; McKenna, R.; Kilberg, M.S.
Asparagine synthetase function, structure, and role in disease
J. Biol. Chem.
292
19952-19958
2017
Homo sapiens (P08243), Escherichia coli (P22106)
Manually annotated by BRENDA team
Zhang, J.; Fan, J.; Venneti, S.; Cross, J.R.; Takagi, T.; Bhinder, B.; Djaballah, H.; Kanai, M.; Cheng, E.H.; Judkins, A.R.; Pawel, B.; Baggs, J.; Cherry, S.; Rabinowitz, J.D.; Thompson, C.B.
Asparagine plays a critical role in regulating cellular adaptation to glutamine depletion
Mol. Cell
56
205-218
2014
Homo sapiens
Manually annotated by BRENDA team