2.7.1.167: D-glycero-beta-D-manno-heptose-7-phosphate kinase

This is an abbreviated version!
For detailed information about D-glycero-beta-D-manno-heptose-7-phosphate kinase, go to the full flat file.

Reaction

Synonyms

bifunctional D-beta-D-heptose-7-phosphate kinase/D-beta-dheptose-1-phosphate adenylyltransferase, D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase, D-beta-D-heptose 7-phosphotransferase, D-beta-D-heptose-7-phosphate kinase, glycero-manno-heptose 7-phosphate kinase, heptose 7-phosphate kinase, HldE, HldE1 heptokinase

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.1 Phosphotransferases with an alcohol group as acceptor

                2.7.1.167 D-glycero-beta-D-manno-heptose-7-phosphate kinase

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Results	in table
9003	AA Sequence
3	Cloned(Commentary)
1	Cofactor
1	Crystallization (Commentary)
2	IC50 Value
2	Inhibitors
1	Metals/Ions
3	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
10	Organism
3	Pathway
8	PDB ID
1	pH Optimum
5	Protein Variants
1	Purification (Commentary)
1	Reaction
10	Reference
15	Substrates and Products (Substrate)
4	Subunits
8	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Engineering

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Engineering on EC 2.7.1.167 - D-glycero-beta-D-manno-heptose-7-phosphate kinase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D264E

Escherichia coli

P76658

loss of activity

698570

D264N

Escherichia coli

P76658

loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure

698570

E198D

Escherichia coli

P76658

loss of enzymatic activity in the mutant protein is not caused by drastic alterations in protein structure

698570

N195D

Escherichia coli

P76658

loss of activity

698570

additional information

Escherichia coli

-

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

737835