Literature summary for 5.3.1.5 extracted from

Jenkins, J.; Janin, J.; Rey, F.; Chiadmi, M.; van Tilbeurgh, H.; Lasters, I.; de Maeyer, M.; van Belle, D.; Wodak, S.J.; Lauwereys, M.; Stanssens, P.; Mrabet, N.T.; Snauwaert, J.; Matthyssens, G.; Lambeir, A.M.
Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites (1992), Biochemistry, 31, 5449-5458.

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Cloned(Commentary)

Cloned (Comment)	Organism
wild-type and mutant enzymes, overexpression in Escherichia coli	Actinoplanes missouriensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of a number of binary and ternary complexes involving wild-type and mutant enzymes, the divalent cations Mg2+, Co2+, or Mn2+ and either the substrate xylose or substrate analogs	Actinoplanes missouriensis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
4.8	-	D-xylose	wild-type enzyme	Actinoplanes missouriensis
16	-	D-xylose	D-xylose, mutant H220Q	Actinoplanes missouriensis
48	-	D-xylose	mutant D257E	Actinoplanes missouriensis
49	-	D-xylose	mutant D257N	Actinoplanes missouriensis
50	-	D-fructose	D-xylose, mutant E181Q	Actinoplanes missouriensis
66	-	D-xylose	mutant D255N	Actinoplanes missouriensis
73	-	D-xylose	mutant E181D	Actinoplanes missouriensis
290	-	D-glucose	wild-type enzyme	Actinoplanes missouriensis
300	-	D-glucose	mutant D257N	Actinoplanes missouriensis
400	-	D-glucose	D-glucose, mutant H220Q	Actinoplanes missouriensis
500	-	D-glucose	mutant H220N	Actinoplanes missouriensis
2400	-	D-glucose	mutant E181D	Actinoplanes missouriensis
5800	-	D-glucose	mutant D257E	Actinoplanes missouriensis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	-	Actinoplanes missouriensis
Mg2+	Mg2+, Mn2+ or Co2+ required for maximal activity	Actinoplanes missouriensis
Mn2+	Mg2+, Mn2+ or Co2+ required for maximal activity	Actinoplanes missouriensis
additional information	two metal sites: metal site 1 is four-coordinated and tetrahedral in the absence of substrate and is six-coordinated and octahedral in its presence, the O2 and O4 atoms of the linear inhibitors and substrate bind to the metal 1. Metal site 2 is octahedral in all cases, its position changes by 0.7 A when it binds O1 of the substrate and by more than 1 A when it also binds O2	Actinoplanes missouriensis

Organism

Organism	UniProt	Comment	Textmining
Actinoplanes missouriensis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-Glucose	-	Actinoplanes missouriensis	D-Fructose	-	?
D-Xylose	-	Actinoplanes missouriensis	D-Xylulose	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.05	-	D-xylose	mutant H220N	Actinoplanes missouriensis
0.08	-	D-xylose	mutant E217S	Actinoplanes missouriensis
0.1	-	D-xylose	mutant E181Q	Actinoplanes missouriensis
0.2	-	D-glucose	mutant H220N	Actinoplanes missouriensis
0.5	-	D-xylose	mutant D255N	Actinoplanes missouriensis
0.6	-	D-xylose	mutant H220Q	Actinoplanes missouriensis
0.7	-	D-glucose	mutant H220Q	Actinoplanes missouriensis
0.9	-	D-xylose	mutant D257N	Actinoplanes missouriensis
1.5	-	D-xylose	mutant E181D	Actinoplanes missouriensis
3.4	-	D-xylose	mutant D257E	Actinoplanes missouriensis
5	-	D-glucose	mutant D257N	Actinoplanes missouriensis
9.3	-	D-glucose	mutant E181D	Actinoplanes missouriensis
17.3	-	D-xylose	wild-type enzyme	Actinoplanes missouriensis
17.7	-	D-glucose	mutant D257E	Actinoplanes missouriensis
24.9	-	D-glucose	wild-type enzyme	Actinoplanes missouriensis

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Release 2023.1 (January 2023)