6.3.5.4: asparagine synthase (glutamine-hydrolysing)
This is an abbreviated version!
For detailed information about asparagine synthase (glutamine-hydrolysing), go to the full flat file.
Word Map on EC 6.3.5.4
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6.3.5.4
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leukemia
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lymphoblastic
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children
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remission
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vincristine
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lymphoma
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methotrexate
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l-asparagine
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prednisone
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cyclophosphamide
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marrow
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erwinia
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daunorubicin
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doxorubicin
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relapsed
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cr
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dexamethasone
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consolidation
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thrombosis
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l-aspartic
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chrysanthemi
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etoposide
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pegylated
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reinduction
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thromboembolism
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cytarabine
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antileukemic
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glutaminase
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intrathecal
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prophylaxis
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non-hodgkin
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ifosfamide
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event-free
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arabinoside
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antithrombin
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carotovora
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6-mercaptopurine
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extranodal
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philadelphia
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agriculture
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lymphosarcoma
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smile
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medicine
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multiagent
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myelosuppression
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hypofibrinogenemia
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standard-risk
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pseudocysts
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nutrition
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teniposide
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drug development
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analysis
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daunomycin
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epipodophyllotoxins
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idarubicin
- 6.3.5.4
- leukemia
- lymphoblastic
- children
-
remission
- vincristine
- lymphoma
- methotrexate
- l-asparagine
- prednisone
- cyclophosphamide
- marrow
- erwinia
- daunorubicin
- doxorubicin
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relapsed
- cr
- dexamethasone
-
consolidation
- thrombosis
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l-aspartic
- chrysanthemi
- etoposide
-
pegylated
-
reinduction
- thromboembolism
- cytarabine
-
antileukemic
- glutaminase
-
intrathecal
-
prophylaxis
-
non-hodgkin
- ifosfamide
-
event-free
-
arabinoside
- antithrombin
- carotovora
- 6-mercaptopurine
-
extranodal
-
philadelphia
- agriculture
- lymphosarcoma
-
smile
- medicine
-
multiagent
-
myelosuppression
- hypofibrinogenemia
-
standard-risk
- pseudocysts
- nutrition
- teniposide
- drug development
- analysis
- daunomycin
- epipodophyllotoxins
- idarubicin
Reaction
Synonyms
AS, AS-A, AS-B, AS1, ASN3, AsnA, ASNase, AsnB, ASNS, AsnS1, AsnS2, AsnS3, AsnS4, asparagine amidotransferase, Asparagine synthetase, Asparagine synthetase (glutamine hydrolyzing), Asparagine synthetase (glutamine), Asparagine synthetase (glutamine-hydrolysing), asparagine synthetase 1, asparagine synthetase 2, Asparagine synthetase A, Asparagine synthetase B, asparagine synthetase, glutamine-dependent, asparagine synthetase1, asparagine synthetase2, At5g10240, bacterial type asparagine synthetase A, CaAS1, glutamine-dependent amidotransferase, Glutamine-dependent asparagine synthetase, HvAS1 protein, HvAS2 protein, HvASN1, HvASN2, HvASN3, HvASN4, HvASN5, L-asparaginase, L-Asparagine synthetase, LDBPK_300470, LiAS-A, MLOC_37219, MLOC_44080, MLOC_63089, MLOC_72774, MLOC_75057, More, NAS2, Os03g0291500, Os06g0265000, OsAS1, OsAS2, PVAS1 protein, PVAS2, Ste10, Synthetase, Asn (glutamine), TaASN1, TaASN2, TaASN4, TaSN1, TaSN2, TS11 cell cycle control protein, type -II asparagine synthetase, type I asparagine synthetase, type II asparagine synthetase
ECTree
6.3.5.4 asparagine synthase (glutamine-hydrolysing)Advanced search results
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results (Engineering
Engineering on EC 6.3.5.4 - asparagine synthase (glutamine-hydrolysing)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C1A
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replacement of Cys1 by either Ala or Ser results in a loss of glutaminase activity and Gln-dependent activity, without any significant effect upon NH4+-dependent Asn synthesis. Kinetic parameters of the NH4+-dependent activity of H29A and H80A are unchanged with respect to wild-type AS-B, the apparent Km for Gln is increased by a factor of 4.5 in Gln-dependent Asn synthesis
C1S
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replacement of Cys1 by either Ala or Ser results in a loss of glutaminase activity and Gln-dependent activity, without any significant effect upon NH4+-dependent Asn synthesis. Kinetic parameters of the NH4+-dependent activity of H29A and H80A are unchanged with respect to wild-type AS-B, the apparent Km for Gln is increased by a factor of 4.5 in Gln-dependent Asn synthesis
E348A
E348D
E348Q
N74A
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mutant N74A, in which Asn is replaced by Ala can also use NH2OH as an alternative substrate to NH4+ and catalyze the hydrolysis of L-glutamic acid gamma-monohydroxamate
N74D
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replacement of the catalytically important residue Asn-74 by Asp, N74D, in the N-terminal domain of Escherichia coli Asn synthetase B confers nitrile hydratase activity upon the mutant enzyme. While wild-type As-B can efficiently catalyze the hydrolysis of Gln to Glu, the N74D As-B mutant exhibits very low glutaminase activity
N74X
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overexpression of a series of mutant enzymes. Site-directed mutagenesis of Asn74 shows that this residue plays a role in catalysis of nitrogen transfer from Gln. Replacement of Arg-30 by an Ala residue yields a mutant enzyme for which the apparent Km for Gln is increased in the Gln-dependent synthesis of Asn. In addition ATP-dependent stimulation of the glutaminase activity is modified or completely eliminated when Arg-30 is replaced by other amino acids
R30A
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overexpression of a series of mutant enzymes. Site-directed mutagenesis of Asn74 shows that this residue plays a role in catalysis of nitrogen transfer from Gln. Replacement of Arg-30 by an Ala residue yields a mutant enzyme for which the apparent Km for Gln is increased in the Gln-dependent synthesis of Asn. In addition ATP-dependent stimulation of the glutaminase activity is modified or completely eliminated when Arg-30 is replaced by other amino acids
R325A
R325L
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
T322X
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
T323X
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
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
C1A
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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
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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
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
up
gene PpAS2 expression is upregulated during drought, but the level of PpAS2 transcripts is not altered by darkness
additional information
E348A
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mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP, but is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source
E348A
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mutant shows similar glutaminase activity to the wild-type enzyme in the absence of ATP, mutant is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source, mutant shows no synthetase activity, ATP-dependent stimulation of glutaminase activity is less than that of wild-type enzyme
E348D
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mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP and is capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source. Formation of the beta-aspartyl-AMP intermediate, and therefore the eventual production of asparagine, is dependent on the presence of a carboxylate side chain at this position in the synthetase active site. In addition, E348 may also play a role in mediating the conformational changes needed to coordinate, albeit weakly, the glutaminase and synthetase activities of the enzyme and to establish the structural integrity of the intramolecular tunnel along which ammonia is translocated
E348D
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mutant shows similar glutaminase activity to the wild-type enzyme in the absence of ATP, mutant is capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source, glutaminase activity of the E348D mutant is stimulated more than 6fold relative to wild-type by the presence of 5 mM ATP, a 5fold decrease in the Km value for aspartate is observed for both the glutamine- and ammonia-dependent synthetase reactions, together with a kcat that is half of that observed for the wildtype enzyme
E348Q
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mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP, but is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source
E348Q
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mutant shows similar glutaminase activity to the wild-type enzyme in the absence of ATP, mutant is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source, mutant shows no synthetase activity, ATP-dependent stimulation of glutaminase activity is less than that of wild-type enzyme
R325A
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
R550C
naturally occuring mutation, causes a decrease in side chain length likely to result in loss of interactions
R550C
naturally occuring mutation, homozygous mutation, causes a decrease in side chain length likely to result in loss of interactions
additional information
phenotypes of isozyme ASN3 knockout mutant lines asn3-1 (SALK_053490) and asn3-2 (SALK_074279), The level of ASN3 mRNA is reduced to 2.5% and 15% of the wild-type value in the seeds of asn3-1 and asn3-2, respectively, overview. Impact of ASN3 disruption on asparagine, glutamine, aspartate and glutamate levels in asn3-1 siliques and compared to wild-type: The young siliques of the asn3-1 knockout line show an increase in glutamine (Glnasn3-1 to GlnCol-0 ratio of 1.014), glutamate (Gluasn3-1 to GluCol-0 ratio of 1.189) and aspartate (Aspasn3-1 to AspCol-0 ratio of 1.149) and a decrease in asparagine (Asnasn3-1 to AsnCol-0 ratio of 0.902)
additional information
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phenotypes of isozyme ASN3 knockout mutant lines asn3-1 (SALK_053490) and asn3-2 (SALK_074279), The level of ASN3 mRNA is reduced to 2.5% and 15% of the wild-type value in the seeds of asn3-1 and asn3-2, respectively, overview. Impact of ASN3 disruption on asparagine, glutamine, aspartate and glutamate levels in asn3-1 siliques and compared to wild-type: The young siliques of the asn3-1 knockout line show an increase in glutamine (Glnasn3-1 to GlnCol-0 ratio of 1.014), glutamate (Gluasn3-1 to GluCol-0 ratio of 1.189) and aspartate (Aspasn3-1 to AspCol-0 ratio of 1.149) and a decrease in asparagine (Asnasn3-1 to AsnCol-0 ratio of 0.902)
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additional information
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various mutant strains, deletion of asnO or asnH, singly or in combination, has no effect on growth rates in media with or without asparagine, deletion of asnB leads to a slow-growth phenotype, even in the presence of asparagine, strains lacking asnO cannot sporulate
additional information
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various mutant strains, deletion of asnO or asnH, singly or in combination, has no effect on growth rates in media with or without asparagine, deletion of asnB leads to a slow-growth phenotype, even in the presence of asparagine, strains lacking asnO cannot sporulate
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additional information
RNA interference is used to silence BmASNS expression in silkworm cells
additional information
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the replacement of the N-terminal Cys by Ala results in the loss of the Gln-dependent Asn synthetase activity, while the NH4+-dependent activity remains unaffected
additional information
identification of two naturally occuring nonsense mutations, R407* and W541Cfs*5 (frameshift mutation), leading to truncated enzyme mutants
additional information
gene deletion mutations of gene asnA are attempted via targeted gene replacement. Gene deletion of LdASNA leads to growth delay in mutants. Chromosomal null mutants of LdASNA cannot be obtained as the double transfectant mutants show aneuploidy
additional information
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gene deletion mutations of gene asnA are attempted via targeted gene replacement. Gene deletion of LdASNA leads to growth delay in mutants. Chromosomal null mutants of LdASNA cannot be obtained as the double transfectant mutants show aneuploidy
additional information
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gene deletion mutations of gene asnA are attempted via targeted gene replacement. Gene deletion of LdASNA leads to growth delay in mutants. Chromosomal null mutants of LdASNA cannot be obtained as the double transfectant mutants show aneuploidy
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additional information
generation of a AS-A gene knockout mutant by targeted gene replacement
additional information
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generation of a AS-A gene knockout mutant by targeted gene replacement
additional information
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generation of a AS-A gene knockout mutant by targeted gene replacement
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additional information
construction of an OsAS1 knockout mutant by insertion of retrotransposon Tos17
additional information
construction of an OsAS1 knockout mutant by insertion of retrotransposon Tos17
additional information
PvAs3 is able to complement Escherichia coli asparagine auxotroph strain ER
additional information
PpAS2 transcript abundance is not affected by any nitrogen treatments or by water stress, PpAS2 expression is essentially constitutive
additional information
PpAS2 transcript abundance is not affected by any nitrogen treatments or by water stress, PpAS2 expression is essentially constitutive
additional information
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PpAS2 transcript abundance is not affected by any nitrogen treatments or by water stress, PpAS2 expression is essentially constitutive
additional information
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design of a silencing construct that simultaneously targets the expression of both isoforms StAs1and StAs2. Tubers of the transformed intragenic plants contain up to 20fold reduced levels of free asparagine. This coincides with a small increase in the formation of glutamine and does not affect tuber shape or yield. Heat-processed products derived from the low-asparagine tubers are indistinguishable from their untransformed counterparts in terms of sensory characteristics. However, both French fries and potato chips accumulate as little as 5% of the acrylamide present in wild-type controls
additional information
after ste10 gene knock-out, the monosaccharide composition of the exopolysaccharide produced by the mutant is changed in comparison with that of native exopolysaccharide Ebosin while its antagonist activity for IL-1R decreases significantly
additional information
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variety Chinese Spring lacks a TaASN2 gene in the B genome
additional information
variety Chinese Spring lacks a TaASN2 gene in the B genome
additional information
variety Chinese Spring lacks a TaASN2 gene in the B genome
