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Ligand UDP-2-acetamido-2-deoxy-alpha-D-glucuronate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.136

UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O = UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+

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1.1.1.136

UDP-N-acetyl-D-glucosamine + NAD+ + H2O = UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADH

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1.1.1.136

2 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

1.1.1.335

UDP-2-acetamido-2-deoxy-alpha-D-glucuronate + NAD+ = UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+

718891, 718852

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4.1.1.B4

UDP-N-acetylglucosaminuronic acid = UDP-N-acetylxylosamine + CO2

712456

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Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.136

UDP-N-acetyl-D-glucosamine + 2 NAD+ + H2O = UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + 2 NADH + 2 H+

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1.1.1.136

UDP-N-acetyl-D-glucosamine + NAD+ + H2O = UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADH

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1.1.1.136

UDP-N-acetyl-D-glucosamine + NADP+ = UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate + NADPH

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1.1.1.136

3 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (5 results)

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Show Turnover Number (5 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.335

0.00031

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25°C, pH 8.5

718891

1.1.1.335

0.00076

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presence of transaminase WlbC, 25°C, pH 8.5

718891

1.1.1.335

0.0039

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presence of transaminase WlbC, 25°C, pH 8.5

718891

1.1.1.335

0.0047

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25°C, pH 8.5

718891

1.1.1.335

4 entries

4.1.1.B4

0.47

-

pH 8.2, 37°C

712456

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.335

0.0056

-

presence of transaminase WlbC, 25°C, pH 8.5

718891

1.1.1.335

0.015

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presence of transaminase WlbC, 25°C, pH 8.5

718891

1.1.1.335

1.1

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25°C, pH 8.5

718891

1.1.1.335

2.36

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25°C, pH 8.5

718891

1.1.1.335

4 entries

4.1.1.B4

0.067

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pH 8.2, 37°C

712456

References & Links

Literature References (3)

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Show Reference (3 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

712456

20529859

Biosynthesis of a new UDP-sugar, UDP-2-acetamido-2-deoxyxylose, in the human pathogen Bacillus cereus subspecies cytotoxis NVH 391-98

2010

Gu, X.; Glushka, J.; Lee, S.G.; Bar-Peled, M.

J. Biol. Chem.

285

24825-24833

718852

19348502

Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1

2009

Larkin, A.; Imperiali, B.

Biochemistry

48

5446-5455

718891

21241053

Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: Enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid

2011

Thoden, J.; Holden, H.

Biochemistry

50

1483-1491

Links to other databases for UDP-2-acetamido-2-deoxy-alpha-D-glucuronate

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Show Links (1 entry)

ChEBI

PubChem

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