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Ligand Butyryl-N-acetyl-cysteamine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.180

de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) butanethioate = [(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl butanoate + N-(2-sulfanylethyl)acetamide

755683

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2.3.1.238

butanoyl-N-acetylcysteamine + monacolin J = (1S,3R,7S,8S,8aR)-8-[2-[(2R,4R)-4-hydroxy-6-oxotetrahydro-2H-pyran-2-yl]ethyl]-3,7-dimethyl-1,2,3,7,8,8a-hexahydronaphthalen-1-yl butanoate + N-acetylcysteamine

729573

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3.1.2.20

N-acetylcysteamine butyrate = N-acetylcysteamine + butyrate

695787

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Product in Enzyme-catalyzed Reactions (5 results)

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Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.10

crotonyl-N-acetyl-cysteamine + NADPH + H+ = butyryl-N-acetyl-cysteamine + NADP+

0

-

1.3.1.10

crotonyl-N-acetyl-cysteamine + NADPH = butyryl-N-acetyl-cysteamine + NADP+

390504, 390497

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1.3.1.10

2 entries

1.3.1.104

crotonyl-N-acetylcysteamine + NADPH + H+ = butyryl-N-acetylcysteamine + NADP+

0

-

1.3.1.39

crotonyl-N-acetyl-cysteamine + NADPH = butyryl-N-acetyl-cysteamine + NADP+

390763, 390762

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1.3.1.9

crotonyl-N-acetyl-cysteamine + NADH = butyryl-N-acetyl-cysteamine + NAD+

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.2.20

1.817

-

at pH 7.5, 30°C

695787

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

3.1.2.20

56

-

at pH 7.5, 30°C

695787

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

390497

-

Stereochemical course of hydrogen transfer catalysed be the enoyl reductase enzyme of the yeast fatty acid synthethase

1980

Sedgwick, B.; Morris, C.

J. Chem. Soc. Chem. Commun.

1980

96-97

390504

10671494

Inhibition of the Staphylococcus aureus NADPH-dependent enoyl-acyl carrier protein reductase by triclosan and hexachlorophene

2000

Heath, R.J.; Li, J.; Roland, G.E.; Rock, C.O.

J. Biol. Chem.

275

4654-4659

390762

4394955

Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis

1970

Dugan, R.E.; Slakey, L.L.; Porter, J.W.

J. Biol. Chem.

245

6312-6316

390763

3535882

Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase

1986

Leanz, G.F.; Hammes, G.G.

Biochemistry

25

5617-5624

695787

19074611

Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate

2009

Kotowska, M.; Pawlik, K.; Smulczyk-Krawczyszyn, A.; Bartosz-Bechowski, H.; Kuczek, K.

Appl. Environ. Microbiol.

75

887-896

729573

17113998

Biosynthesis of lovastatin analogs with a broadly specific acyltransferase

2006

Xie, X.; Watanabe, K.; Wojcicki, W.A.; Wang, C.C.; Tang, Y.

Chem. Biol.

13

1161-1169

755683

28060484

A highly promiscuous beta-ketoacyl-ACP synthase (KAS) III-like protein is involved in pactamycin biosynthesis

2017

Abugrain, M.E.; Brumsted, C.J.; Osborn, A.R.; Philmus, B.; Mahmud, T.

ACS Chem. Biol.

12

362-366

Links to other databases for Butyryl-N-acetyl-cysteamine

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Show Links (1 entry)

ChEBI

PubChem

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