Literature summary for 2.7.1.167 extracted from

Li, T.; Wen, L.; Williams, A.; Wu, B.; Li, L.; Qu, J.; Meisner, J.; Xiao, Z.; Fang, J.; Wang, P.G.
Chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose and study of the substrate specificity of HldE (2014), Bioorg. Med. Chem., 22, 1139-1147.

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Protein Variants

Protein Variants	Comment	Organism
additional information	development of an efficient one-pot three enzymes strategy for chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose (ADP-D, D-heptose) using chemically synthesized D,D-heptose-7-phosphate and the ADP-D,D-heptose biosynthetic enzymes HldE and GmhB, method, overview	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-glycero-D-manno-heptose 7-phosphate + ATP	Escherichia coli	exclusively forming the beta-anomer, namely, D-glycero-beta-D-manno-heptose-1,7-bisphosphate	D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7-O-phosphono-6-deoxy-glycero-D-manno-heptopyranosyl phosphate + ATP	low activity	Escherichia coli	? + ADP	-	?
7-phosphate-D-glycero-beta-D-manno-heptose + ATP	-	Escherichia coli	D-glycero-D-manno-beta-heptose 1,7-bisphosphate + ADP	-	?
D-glycero-D-manno-heptose 7-phosphate + ATP	exclusively forming the beta-anomer, namely, D-glycero-beta-D-manno-heptose-1,7-bisphosphate	Escherichia coli	D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP	-	?
D-glycero-D-manno-heptose 7-phosphate + ATP	anomeric phosphorylation by the kinase activity of HldE exclusively forming the beta-anomer, namely, D-glycero-beta-D-manno-heptose-1,7-bisphosphate	Escherichia coli	D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP	-	?
additional information	HldE has highly restricted substrate specificity towards structurally modified heptose-7-phosphate analogues, substrate specificity of enzyme HldE, overview. No activity with D,L-glycero-D-manno-heptose, mannose 6-phosphate, 7-O-phosphono-L-glycero-D-manno-heptopyranosyl phosphate, and 7-O-sulfo-D-glycero-D-manno-heptopyranoside	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
HldE	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)