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Literature summary for 6.3.5.4 extracted from

  • Boehlein, S.K.; Richards, N.G.J.; Schuster, S.M.
    Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B (1994), J. Biol. Chem., 269, 7450-7457.
    View publication on PubMed
Search for more literature for 6.3.5.4

Cloned(Commentary)

Cloned (Comment) Organism
and overexpression Escherichia coli

Protein Variants

Protein Variants Comment Organism
C1A 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 Escherichia coli
C1S 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 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Gln inhibitor of the NH4+-dependent reaction catalyzed by both the C1A and C1S mutants of AS-B Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.53
-
 Asp NH4+-dependent activity, wild-type Escherichia coli
0.66
-
 Gln wild-type enzyme Escherichia coli
0.85
-
 Asp Asp, wild-type enzyme, Gln-dependent activity Escherichia coli
17
-
 NH4+ wild-type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ is the only divalent metal ion that can replace Mg2+ with 80% of the Mg2+-dependent AS-B activity activity with Gln and 52% of the Mg2+-dependent AS-B activity with NH4+ Escherichia coli
Mg2+ highest stimulation of divalent metal ions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type and mutant enzymes C1A, C1S, H29A , H80A, D33N, D33E, and A104H
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Asp + L-Gln
-
 Escherichia coli AMP + diphosphate + Asn + Glu
-
 ?
CTP + L-Asp + L-Gln weak activity Escherichia coli CMP + diphosphate + Asn + Glu
-
 ?
dATP + L-Asp + L-Gln utilized at a similar rate as ATP Escherichia coli dAMP + diphosphate + Asn + Glu
-
 ?
dATP + L-Asp + NH3 utilized at a similar rate as ATP Escherichia coli dAMP + diphosphate + Asn
-
 ?
GTP + L-Asp + L-Gln 15% of the activity relative to ATP Escherichia coli GMP + diphosphate + Asn + Glu
-
 ?
additional information no activity with ITP or XTP Escherichia coli ?
-
 ?
UTP + L-Asp + L-Gln weak activity Escherichia coli UMP + diphosphate + Asn + Glu
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 8
-
 Escherichia coli