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Ligand D-glycero-alpha-D-manno-heptose 1,7-bisphosphate

Basic Ligand Information

Molecular Structure

Related pathways

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.83

D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate

700026, 696367

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In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.168

D-glycero-alpha-D-manno-heptose 7-phosphate + ATP = D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + ADP

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-

Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Substrate (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.82

D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate

696368, 696367

-

3.1.3.83

D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate

700026, 696367

-

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.168

D-glycero-alpha-D-manno-heptose 7-phosphate + ATP = D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + ADP

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-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (8 results)

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Show Turnover Number (8 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.3.82

0.0017

-

pH 7.5, 25°C, mutant enzyme C92A

696368

3.1.3.82

0.042

-

pH 7.5, 25°C, mutant enzyme C107A

696368

3.1.3.82

0.057

-

pH 7.5, 25°C, mutant enzyme C109A

696368

3.1.3.82

4.4

-

pH 7.5, 25°C

696367

3.1.3.82

4.6

-

pH 7.5, 25°C

696367

3.1.3.82

4.6

-

pH 7.5, 25°C, wild-type

696368

3.1.3.82

5.9

-

pH 7.5, 25°C

696367

3.1.3.82

7 entries

3.1.3.83

29

-

pH 7.5, 25°C

696367

K_M Value (8 results)

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Show KM Value (8 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.3.82

0.032

-

pH 7.5, 25°C, mutant enzyme C107A

696368

3.1.3.82

0.045

-

pH 7.5, 25°C, mutant enzyme C109A

696368

3.1.3.82

0.067

-

pH 7.5, 25°C

696367

3.1.3.82

0.067

-

pH 7.5, 25°C, wild-type

696368

3.1.3.82

0.28

-

pH 7.5, 25°C

696367

3.1.3.82

0.3

-

pH 7.5, 25°C, mutant enzyme C92A

696368

3.1.3.82

0.58

-

pH 7.5, 25°C

696367

3.1.3.82

7 entries

3.1.3.83

0.033

-

pH 7.5, 25°C

696367

References & Links

Literature References (3)

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Show Reference (3 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

696367

20050615

Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB)

2010

Wang, L.; Huang, H.; Nguyen, H.H.; Allen, K.N.; Mariano, P.S.; Dunaway-Mariano, D.

Biochemistry

49

1072-1081

696368

20050614

Structural determinants of substrate recognition in the HAD superfamily member D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB)

2010

Nguyen, H.H.; Wang, L.; Huang, H.; Peisach, E.; Dunaway-Mariano, D.; Allen, K.N.

Biochemistry

49

1082-1092

700026

12101286

Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides

2002

Valvano, M.A.; Messner, P.; Kosma, P.

Microbiology

148

1979-1989

Links to other databases for D-glycero-alpha-D-manno-heptose 1,7-bisphosphate

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Show Links (1 entry)