Literature summary extracted from

Bausch, C.; Peekhaus, N.; Utz, C.; Blais, T.; Murray, E.; Lowary, T.; Conway, T.
Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonate acid catabolism in Escherichia coli (1998), J. Bacteriol., 180, 3704-3710.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.1.1.264	overexpression in Escherichia coli	Escherichia coli

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.1.1.264	1	-	L-Idonate	-	Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.1.1.264	L-idonate + NAD(P)+	Escherichia coli	specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate	5-dehydrogluconate + NAD(P)H	-	r

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.264	Escherichia coli	P39346	K-12 strains, idnD gene	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.1.1.264	culture condition:L-idonate-grown cell	induction of enzyme synthesis by L-idonate containing culture medium	Escherichia coli	-

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.1.1.264	0.04	-	with NADPH as cofactor	Escherichia coli
1.1.1.264	0.05	-	with NADH as cofactor	Escherichia coli

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.264	L-idonate + NAD(P)+	specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate	Escherichia coli	5-dehydrogluconate + NAD(P)H	-	r

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.1.1.264	NADH	preferred cofactor	Escherichia coli
1.1.1.264	NADPH	less effective than NAD+	Escherichia coli

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Release 2023.1 (January 2023)