Literature summary for 4.1.3.34 extracted from

Man, W.J.; Li, Y.; O'Connor, C.D.; Wilton, D.C.
Conversion of citrate synthase into citryl-CoA lyase as a result of mutation of the active-site aspartic acid residue to glutamic acid (1991), Biochem. J., 280, 521-526.

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Protein Variants

Protein Variants	Comment	Organism
D362E	conversion of citrate synthase, EC 4.1.3.7, into citryl-CoA lyase, EC 4.1.3.34	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0367	-	oxaloacetate	wild-type enzyme	Escherichia coli
0.0565	-	oxaloacetate	mutant enzyme D362E	Escherichia coli
0.0718	-	acetyl-CoA	mutant enzyme D362E	Escherichia coli
0.345	-	acetyl-CoA	wild-type enzyme	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	mutant D362E, conversion of citrate synthase, EC 4.1.3.7, into citryl-CoA lyase, EC 4.1.3.34, as a result of mutation of the active-site Asp to Glu	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(3S)-citryl-CoA	-	Escherichia coli	acetyl-CoA + oxaloacetate	-	?

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Release 2023.1 (January 2023)