• BRENDA home

• Basic Ligand Information
• • Molecular Structure
  • Sum Formula
  • BRENDA Name
  • Synonyms
  • InChIKey
  • Pathways
• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
  • Links

print visible entries

print all entries

Ligand Pantoate

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

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

top print hide

Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.169

ATP + pantoate = ADP + 4-phosphopantoate

704547

-

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

top print hide

Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.169

ketopantoate + NADPH = pantoate + NADP+

286110, 286107,

2ofp, 3D-view

Substrate in Enzyme-catalyzed Reactions (4 results)

top print hide

Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.169

ATP + pantoate = ADP + 4-phosphopantoate

704547, 722549

-

2.7.1.169

CTP + pantoate = CDP + 4-phosphopantoate

722549

-

2.7.1.169

GTP + pantoate = GDP + 4-phosphopantoate

722549

-

2.7.1.169

UTP + pantoate = UDP + 4-phosphopantoate

722549

-

2.7.1.169

4 entries

Product in Enzyme-catalyzed Reactions (10 results)

top print hide

Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.169

ketopantoate + NADPH = pantoate + NADP+

286110, 286107,

2ofp, 3D-view

1.1.1.169

ketopantoic acid + NADH = pantoic acid + NAD+

286107

2ofp, 3D-view

1.1.1.169

ketopantoic acid + NADPH = pantoic acid + NADP+

286107, 286104, 286105

2ofp, 3D-view

1.1.99.30

2-oxo-3,3-dimethyl-4-hydroxybutanoate + reduced benzyl viologen = 3,3-dimethyl-2,4-dihydroxybutanoate + oxidized benzyl viologen

-

-

1.1.99.30

2-oxo-3,3-dimethyl-4-hydroxybutanoate + reduced methyl viologen = 3,3-dimethyl-2,4-dihydroxybutanoate + oxidized methyl viologen

-

-

3.1.1.25

alpha-hydroxy-beta,beta-dimethyl-gamma-butyrolactone + H2O = 2,4-dihydroxy-3,3-dimethylbutanoate

-

-

3.1.1.25

pantoyl lactone + H2O = 2,4-dihydroxy-3,3-dimethylbutanoic acid

-

-

3.1.1.25

DL-pantoyl lactone + H2O = pantoic acid

-

-

3.1.1.25

DL-pantoyllactone + H2O = pantoic acid

-

-

1.1.1.169

3 entries

1.1.99.30

2 entries

3.1.1.25

4 entries

3.5.1.22

pantothenate + H2O = 2,4-dihydroxy-3,3-dimethylbutyric acid + beta-alanine

-

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.169

noncompetitive versus ketopantoate and NADPH

286108

2ofp, 3D-view

2.1.2.11

0.05 mM or above

485700, 485701

-

2.7.1.169

substrate inhibition

722549

-

3D Structure of Enzyme-Ligand-Complex (PDB) (11 results)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (11 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.169

2ofp, 3D-view

6.3.2.1

1n2b, 3D-view

6.3.2.1

1n2e, 3D-view

6.3.2.1

1n2j, 3D-view

6.3.2.1

3guz, 3D-view

6.3.2.1

3q12, 3D-view

6.3.2.1

1n2b, 3D-view

6.3.2.1

1n2e, 3D-view

6.3.2.1

1n2j, 3D-view

6.3.2.1

3guz, 3D-view

6.3.2.1

3q12, 3D-view

6.3.2.1

10 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

top print hide

Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.7.1.169

1.56

-

42°C

704547

2.7.1.169

2.82

-

pH 7.5, 42°C

722549

2.7.1.169

2 entries

K_M Value (3 results)

top print hide

Show KM Value (3 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.169

0.26

-

+/-0.04

286108

2.7.1.169

1.2

-

42°C

704547

2.7.1.169

2.92

-

pH 7.5, 42°C

722549

2.7.1.169

2 entries

K_i Value (1 result)

top print hide

Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.1.169

9.75

-

pH 7.5, 42°C

722549

References & Links

Literature References (9)

top print hide

Show Reference (9 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

286104

-

Separation and preliminary studies on 2-ketopantoyl lactone and 2-ketopantoic acid reductases of yeast

1972

King, H.L.; Wilken, D.R.

J. Biol. Chem.

247

4096-4098

286105

234966

Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate

1975

Wilken, D.R.; King, H.L.; Dyar, R.E.

J. Biol. Chem.

250

2311-2314

286107

9488683

ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway

1998

Frodyma, M.E.; Downs, D.

J. Biol. Chem.

273

5572-5576

286108

10736170

Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase

2000

Zheng, R.; Blanchard, J.S.

Biochemistry

39

3708-3717

286110

11724562

Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism

2001

Matak-Vinkovic, D.; Vinkovic, M.; Saldanha, S.A.; Ashurst, J.L.; von Delft, F.; Inoue, T.; Miguel, R.N.; Smith, A.G.; Blundell, T.L.; Abell, C.

Biochemistry

40

14493-14500

485700

6463

Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties

1976

Powers, S.G.; Snell, E.E.

J. Biol. Chem.

251

3786-3793

485701

374973

Purification and properties of ketopantoate hydroxymethyltransferase

1979

Powers, S.G.; Snell, E.E.

Methods Enzymol.

62

204-209

704547

19666462

Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the archaea

2009

Yokooji, Y.; Tomita, H.; Atomi, H.; Imanaka, T.

J. Biol. Chem.

284

28137-28145

722549

22865846

Biochemical characterization of pantoate kinase, a novel enzyme necessary for coenzyme A biosynthesis in the Archaea

2012

Tomita, H.; Yokooji, Y.; Ishibashi, T.; Imanaka, T.; Atomi, H.

J. Bacteriol.

194

5434-5443

Links to other databases for Pantoate

top print hide

Show Links (1 entry)

ChEBI

PubChem

-