Literature summary for 6.3.5.4 extracted from

Boehlein, S.K.; Walworth, E.S.; Richards, N.G.J.; Schuster, S.M.
Mutagenesis and chemical rescue indicate residues involved in beta-aspartyl-AMP formation by Escherichia coli asparagine synthetase B (1997), J. Biol. Chem., 272, 12384-12392.

Search for more literature for 6.3.5.4

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Km-values of a number of site-specific mutant enzymes	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	wild-type and mutant enzymes, E317A, E317Q, T318A, Y319A, Y319F, D320A, V321A, T322A, T322S, T322V, T322Y, T323A, T323I, T323L, T323S, T323V, R325A, R325K, T328S	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate	Arg325 is involved in stabilization of a pentacovalent intermediate leading to the formation of beta-aspartyl-AMP	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-Asp + L-Gln	-	Escherichia coli	AMP + diphosphate + Asn + Glu	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	turnover-numbers of a number of site-specific AS-B mutant enzymes	Escherichia coli

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Release 2023.1 (January 2023)