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Ligand alpha-maltotriosyl fluoride

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Substrate (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.1

alpha-maltotriosyl fluoride + H2O = maltotriose + fluoride

654643, 664094

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Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.2.1.1

283

-

30°C, pH 7.0

654643

3.2.1.1

285

-

pH 7.0, 30°C

664094

3.2.1.1

2 entries

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

3.2.1.1

0.51

-

30°C, pH 7.0

654643

References & Links

Literature References (2)

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Show Reference (2 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

654643

11914097

Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids

2002

Rydberg, E.H.; Li, C.; Maurus, R.; Overall, C.M.; Brayer, G.D.; Withers, S.G.

Biochemistry

41

4492-4502

664094

15736945

Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts

2005

Li, C.; Begum, A.; Numao, S.; Park, K.H.; Withers, S.G.; Brayer, G.D.

Biochemistry

44

3347-3357

Links to other databases for alpha-maltotriosyl fluoride

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Show Links (1 entry)

ChEBI

PubChem

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