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Ligand pentan-3-ol

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (9 results)

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Show Substrate (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

3-pentanol + NAD+ = 3-pentanone + NADH + H+

697839, 695811

-

1.1.1.1

pentan-3-ol + NAD+ = 3-pentanone + NADH

285586, 285621

-

1.1.1.1

pentan-3-ol + NAD+ = 3-pentanone + NADH + H+

697839

-

1.1.1.1

3 entries

1.1.1.80

pentan-3-ol + NADP+ = pentan-3-one + NADPH + H+

724969

-

1.1.1.B4

3-pentanol + NAD+ = 3-pentanone + NADH

687864

-

1.1.3.18

3-pentanol + O2 = 3-pentanone + H2O2

348181, 287626, 348177, 348180

-

1.1.5.7

3-pentanol + pyrroloquinoline quinone = 3-pentanone + pyrroloquinoline quinol

696803

-

1.1.9.1

3-pentanol + ferricyanide = pentan-3-one + ferrocyanide

705187, 687362

-

1.1.9.1

3-pentanol + ferrocyanide = pentan-3-one + ferricyanide

701774

-

1.1.9.1

2 entries

Product in Enzyme-catalyzed Reactions (9 results)

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Show Product (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

diethylketone + NADH + H+ = 3-pentanol + NAD+

0

-

1.1.1.1

3-pentanone + NADH = pentan-3-ol + NAD+

285586

-

1.1.1.1

3-pentanone + NADPH + H+ = pentan-3-ol + NADP+

0

-

1.1.1.1

3 entries

1.1.1.80

pentan-3-one + NADPH + H+ = pentan-3-ol + NADP+

0

-

1.1.1.B3

pentan-3-one + NADH + H+ = pentan-3-ol + NAD+

0

-

1.1.1.B4

3-pentanone + NAD+ = 3-pentanol + NADH + H+

0

-

1.1.1.B4

3-pentanone + NADH = 3-pentanol + NAD+

0

-

1.1.1.B4

2 entries

1.14.13.230

pentane + NADH + H+ + O2 = pentan-3-ol + NAD+ + H2O

0

-

3.1.6.19

(3R)-pentan-3-yl sulfate + H2O = pentan-3-ol + sulfate

0

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.13

1 mM, 16% inhibition

484911

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.1

1.5

-

wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

697839

1.1.1.1

2.26

-

-

285586

1.1.1.1

2.92

-

-

285621

1.1.1.1

3 entries

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

1.1.1.1

0.225

-

-

285621

1.1.1.1

0.27

-

wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

697839

1.1.1.1

1.6

-

-

285586

1.1.1.1

3 entries

1.1.1.80

0.0015

-

37°C, pH 9.0

724969

1.1.1.B4

0.76

-

pH 8.5, 30°C

687864

1.1.9.1

28

-

enzyme electrode, pH 7.7, presence of CaCl2

701774

1.1.9.1

30

-

pH 7.5, 25°C

705187

1.1.9.1

30

-

soluble enzyme, pH 7.7, presence of CaCl2

701774

1.1.9.1

3 entries

References & Links

Literature References (15)

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Show Reference (15 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

285586

1935957

Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme

1991

Adolph, H.W.; Maurer, P.; Schneider-Bernloehr, H.; Sartorius, C.; Zeppezauer, M.

Eur. J. Biochem.

201

615-625

285621

3115775

A novel archaebacterial NAD+-dependent alcohol dehydrogenase. Purification and properties

1987

Rella, R.; Raia, C.A.; Pensa, M.; Pisani, F.M.; Gambacorta, A.; de Rosa, M.; Rossi, M.

Eur. J. Biochem.

167

475-479

287626

-

Purification and properties of polyvinyl alcohol oxidase with broad substrate range obtained from Pseudomonas vesicularis var. povalolyticus PH

1997

Kawagoshi, Y.; Fujita, M.

World J. Microbiol. Biotechnol.

13

273-277

348177

-

Purification and properties of secondary alcohol oxidase from a strain of Pseudomonas

1979

Morita, M.; Hamada, N.; Sakai, K.; Watanabe, Y.

Agric. Biol. Chem.

43

1225-1235

348180

-

Purification of membrane-bound polyinyl alcohol oxidase in Pseudomonas sp. VM15C

1983

Shimao, M.; Tsuda, T.; Takahashi, M.; Kato, N.; Sakazawa, C.

FEMS Microbiol. Lett.

20

429-433

348181

-

Purification and properties of secondary alcohol oxidase with an acidic isoelectric point

1985

Sakai, K.; Hamada, N.; Watanabe, Y.

Agric. Biol. Chem.

49

817-825

484911

7030206

Microbial oxidation of methanol: properties of crystallized alcohol oxidase from a yeast, Pichia sp

1981

Patel, R.N.; Hou, C.T.; Laskin, A.I.; Derelanko, P.

Arch. Biochem. Biophys.

210

481-488

687362

7730276

Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols

1995

Toyama, H.; Fujii, A.; Matsushita, K.; Shinagawa, E.; Ameyama, M.; Adachi, O.

J. Bacteriol.

177

2442-2450

687864

16233542

Thermostable NAD+-dependent (R)-specific secondary alcohol dehydrogenase from cholesterol-utilizing Burkholderia sp. AIU 652

2003

Isobe, K.; Wakao, N.

J. Biosci. Bioeng.

96

387-393

695811

18704396

TADH, the thermostable alcohol dehydrogenase from Thermus sp. ATN1: a versatile new biocatalyst for organic synthesis

2008

Hoellrigl, V.; Hollmann, F.; Kleeb, A.C.; Buehler, K.; Schmid, A.

Appl. Microbiol. Biotechnol.

81

263-273

696803

11826975

Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9

2001

Moonmangmee, D.; Fujii, Y.; Toyama, H.; Theeragool, G.; Lotong, N.; Matsushita, K.; Adachi, O.

Biosci. Biotechnol. Biochem.

65

2763-2772

697839

19588068

Role of Tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase

2009

Pennacchio, A.; Esposito, L.; Zagari, A.; Rossi, M.; Raia, C.A.

Extremophiles

13

751-761

701774

-

Enantioselective oxidation of secondary alcohols at a quinohemoprotein alcohol dehydrogenase electrode

1999

Somers, W.A.C.; Stigter, E.C.A.; Van Hartingsveldt, W.; Van Der Lugt, J.P.

Appl. Biochem. Biotechnol.

75

151-161

705187

-

Enantioselective oxidation of secondary alcohols by quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni

1997

Stigter, E.C.A.; van der Lugt, J.P.; Somers, W.A.C.

J. Mol. Catal. B

2

291-297

724969

22686835

Secondary alcohol dehydrogenase catalyzes the reduction of exogenous acetone to 2-propanol in Trichomonas vaginalis

2012

Sutak, R.; Hrdy, I.; Dolezal, P.; Cabala, R.; Sedinova, M.; Lewin, J.; Harant, K.; Mueller, M.; Tachezy, J.

FEBS J.

279

2768-2780

Links to other databases for pentan-3-ol

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Show Links (1 entry)

ChEBI

PubChem