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Ligand maltose 1-phosphate

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

2.4.99.16

alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n = phosphate + [(1->4)-alpha-D-glucosyl]n+2

717816, 737691, 759476

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In Vivo Product in Enzyme-catalyzed Reactions (4 results)

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.342

ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate = ADP + alpha-maltose-1-phosphate

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-

2.7.1.175

ATP + maltose = ADP + alpha-maltose 1-phosphate

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-

2.7.1.175

ATP + maltose = ADP + alpha-maltose-1-phosphate

-

-

2.7.1.175

ATP + maltose = ADP + maltose 1-phosphate

-

-

2.7.1.175

3 entries

Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Substrate (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.99.16

alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n = phosphate + [(1->4)-alpha-D-glucosyl]n+2

717816, 737691, 759476

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3.1.3.23

alpha-maltose 1-phosphate + H2O = alpha-maltose + phosphate

94723

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Product in Enzyme-catalyzed Reactions (7 results)

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Show Product (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.342

ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate = ADP + alpha-maltose-1-phosphate

-

-

2.7.1.175

ATP + maltose = ADP + alpha-maltose 1-phosphate

-

-

2.7.1.175

ATP + maltose = ADP + alpha-maltose-1-phosphate

-

-

2.7.1.175

ATP + maltose = ADP + maltose 1-phosphate

-

-

2.7.1.175

GTP + maltose = GDP + maltose 1-phosphate

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-

2.7.1.175

UTP + maltose = UDP + maltose 1-phosphate

-

-

2.7.1.175

5 entries

2.7.7.36

ADP-maltose + phosphate = ADP + maltose 1-phosphate

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-

Enzyme Kinetic Parameters

K_M Value (1 result)

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Show KM Value (1 entry)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.3.23

2.2

-

-

94723

References & Links

Literature References (5)

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Show Reference (5 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

94723

-

Molecular weight and some physicochemical and catalytic properties of sugar phosphate phosphohydrolase from Escherichia coli and Neisseria meningitidis

1975

Lee, Y.P.; Lee, A.T.; Choy, F.Y.M.; Sowokinos, J.R.

J. Biol. Chem.

250

3729-3737

717816

20118231

Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen

2010

Elbein, A.D.; Pastuszak, I.; Tackett, A.J.; Wilson, T.; Pan, Y.T.

J. Biol. Chem.

285

9803-9812

737691

24689960

Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds alpha-maltose 1-phosphate and forms a maltosyl-enzyme intermediate

2014

Syson, K.; Stevenson, C.E.; Rashid, A.M.; Saalbach, G.; Tang, M.; Tuukkanen, A.; Svergun, D.I.; Withers, S.G.; Lawson, D.M.; Bornemann, S.

Biochemistry

53

2494-2504

759476

27531751

Ligand-bound structures and site-directed mutagenesis identify the acceptor and secondary binding sites of Streptomyces coelicolor maltosyltransferase GlgE

2016

Syson, K.; Stevenson, C.E.; Miah, F.; Barclay, J.E.; Tang, M.; Gorelik, A.; Rashid, A.M.; Lawson, D.M.; Bornemann, S.

J. Biol. Chem.

291

21531-21540

759476

27531751

Ligand-bound structures and site-directed mutagenesis identify the acceptor and secondary binding sites of Streptomyces coelicolor maltosyltransferase GlgE

2016

Syson, K.; Stevenson, C.E.; Miah, F.; Barclay, J.E.; Tang, M.; Gorelik, A.; Rashid, A.M.; Lawson, D.M.; Bornemann, S.

J. Biol. Chem.

291

21531-21540

759476

2 entries

Links to other databases for maltose 1-phosphate

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Show Links (1 entry)