Literature summary for 7.5.2.8 extracted from

Castano, D.; Millet, O.
Backbone chemical shifts assignments of D-allose binding protein in the free form and in complex with D-allose (2011), Biomol. NMR Assign., 5, 31-34 .

Search for more literature for 7.5.2.8

Crystallization (Commentary)

Crystallization (Comment)	Organism
D-allose binding protein in the free form and in complex with D-allose	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	contains zinc	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + D-allose-[allose-binding protein][side 1]	Escherichia coli	-	ADP + phosphate + D-allose[side 2] + [allose-binding protein][side 1]	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Q-Sepharose column chromatography and Superdex 75 gel filtration	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + D-allose-[allose-binding protein][side 1]	-	Escherichia coli	ADP + phosphate + D-allose[side 2] + [allose-binding protein][side 1]	-	?
additional information	D-allose binding protein can function as a low affinity transporter for D-ribose	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
?	x * more than 30000, subunit ALBP, calculated from amino acid sequence	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ALBP	-	Escherichia coli
D-allose binding protein	subunit of the D-allose ABC transporter system	Escherichia coli

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Release 2023.1 (January 2023)