Information on EC 6.3.1.1 - aspartate-ammonia ligase

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

EC NUMBER
COMMENTARY hide
6.3.1.1
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RECOMMENDED NAME
GeneOntology No.
aspartate-ammonia ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid amide hydrolysis
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carboxylic
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
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Biosynthesis of secondary metabolites
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Cyanoamino acid metabolism
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L-asparagine biosynthesis II
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Metabolic pathways
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NIL
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aspartate and asparagine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate:ammonia ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-69-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the organism contains both enzymes EC 6.3.1.1. and EC 6.3.5.4: The gene asnA codes for ammonia-dependent asparagine synthetases, EC 6.3.1.1, and the gene asnB codes for Gln-dependent asparagine synthetase, EC 6.3.5.4
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Manually annotated by BRENDA team
strain JW 79/3
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Manually annotated by BRENDA team
strain JW 79/3
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-Asp + hydroxylamine
AMP + diphosphate + Asn + beta-aspartyl hydroxamate
show the reaction diagram
ATP + L-Asp + NH4+
AMP + diphosphate + Asn
show the reaction diagram
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
show the reaction diagram
additional information
?
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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-aspartate + NH3
AMP + diphosphate + L-asparagine
show the reaction diagram
additional information
?
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importance of ASNS protein in the cellular mechanisms that confer drug resistance upon the leukemic cells
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenylated sulfoximine
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diphosphate
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iodoacetamide
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L-Asp
N-ethylmaleimide
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p-mercuribenzoate
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sulfoximine
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poor inhibitor
additional information
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CHOP suppresses the induction of the endogenous ASNS gene and inhibits transcription from a reporter gene driven by the ASNS promoter following activation by ATF4 or amino acid deprivation. The inhibitory effect of CHOP on the ASNS gene is not observed when truncated proteins, encoding either the N- or C-terminal portion of the protein, are expressed, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phytohemagglutinin
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 2
ATP
4.2 - 26
L-Asp
4
NH4+
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ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000067
adenylated sulfoximine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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an NCI cell line
Manually annotated by BRENDA team
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leukemia-derived camcer cell line
Manually annotated by BRENDA team
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leukemia-derived camcer cell line
Manually annotated by BRENDA team
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mass spectrometric quantification of asparagine synthetase in circulating leukemia cells from acute lymphoblastic leukemia patients, method development and optimization, overview
Manually annotated by BRENDA team
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leukemia-derived camcer cell line
Manually annotated by BRENDA team
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leukemia-derived camcer cell line
Manually annotated by BRENDA team
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enzyme expression analysis in 19 human ovarian cell lines, overview
Manually annotated by BRENDA team
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of the NCI-60 cell line panel
Manually annotated by BRENDA team
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an NCI cell line
Manually annotated by BRENDA team
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an NCI cell line
Manually annotated by BRENDA team
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an NCI cell line
Manually annotated by BRENDA team
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leukemia-derived camcer cell line
Manually annotated by BRENDA team
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leukemia-derived camcer cell line
Manually annotated by BRENDA team
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an NCI cell line
Manually annotated by BRENDA team
additional information
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DNA fingerprinting in ovarian cancer cell lines, overview
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
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gel filtration
82000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
at 2.7 A resolution
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crystal structure of native AsnA and complexed with L-asparagine and AMP at 2.5 A, 2.2 A and 2.2 A resolution, respectively
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crystallized in two different conditions using the hanging-drop vapour-diffusion method. Crystals belonging to space group C2 with unit-cell parameters a = 103.6, b = 43.3, c = 121.5 A, beta = 112.6° and one dimer per asymmetric unit are obtained in the presence of 2-propanol and PEG 4000 at pH 5.6. Another crystal form is obtained in the presence of dioxan and belongs to the monoclinic space group P2(1), with unit-cell parameters a = 96.8, b = 103.9, c = 98.4 A, beta = 107.5° and two dimers per asymmetric unit. Two different native diffraction data sets are collected to 2.3 A and 3.0 A resolution using synchrotron radiation and cryocooling for crystals belonging to space groups C2 and P2(1), respectively
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sitting-drop vapor diffusion. The fold of this protein is similar to that of bacterial asparagine synthetase A and resembles the catalytic cores of aspartyl-tRNA synthetase and asparaginyl-tRNA synthetase
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol and 2-mercaptoethanol stabilize
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
fusion protein constructed of asparagine synthetase A structural gene fused to the 3“end of the human carbonic anhydrase II structural gene
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bacterial gene is placed under control of light-dependent promoters, and introduced by transformation into Lotus corniculatus plants. The asnA-expressing plants are characterized by premature flowering and reduced growth. Transformation with asnA also induces a significant reduction of photosynthesis when measured under saturated light and ambient CO2 conditions
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expression analysis in HEK-293 cells in response to ATF4 or CHOP
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expression of Escherichia coli asnA gene in Brassica napus could be of advantage at high N supply, but not at limiting N “fertilizer supply
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quantitative enzyme expression analysis in Hep-G2 cells in absence or presence of UPR blockers and activators, transcription factor recruitment to the ASNS promoter during the UPR, transcriptional activation of UPR target genes is mediated by three signaling cascades PERK/eIF2alpha/ATF4, ATF6, and IRE1/XBP1, UPR activation does not trigger increased recruitment of Mediator subunits to the ASNS promoter, the IRE1/XBP1 and ATF6 branches of the UPR do not participate in the induction of ASNS transcription, overview
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the enzyme is obtained by means of a plasmid, pUNAd37, a derivative of pUC18 in Escherichia coli. The plasmid is constructed by optimizing a DNA sequence between the promoter and the ribosome binding region
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C315A
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no change in activity, necessary to improve crystallization
C51A
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no change in activity, necessary to improve crystallization
additional information
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asparagine synthetase A structural gene is fused to the 3'-end of the human carbonic anhydrase II structural gene and overexpressed in Escherichia coli
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