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Ligand 2-N-Hexadecanoylamino-4-nitrophenol

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Product in Enzyme-catalyzed Reactions (4 results)

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Show Product (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.4.12

2-(N-hexadecanoylamino)-4-nitrophenylphosphorylcholine + H2O = 2-(N-hexadecanoylamino)-4-nitrophenol + choline phosphate

652444

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3.1.4.12

2-hexadecanoylamino-4-nitrophenylphosphocholine + H2O = 2-hexadecanoylamino-4-nitrophenol + choline phosphate

650502, 651801

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3.1.4.12

2-n-hexadecanoylamino-4-nitrophenylphosphorylcholine + H2O = 2-n-hexadecanoylamino-4-nitrophenol + choline phosphate

0

-

3.1.4.12

3 entries

3.2.1.123

2-N-hexadecanoylamino-4-nitrophenyl-O-beta-lactoside + H2O = N-(2-hydroxy-5-nitrophenyl)hexadecanamide + beta-lactose

0

-

Enzyme Kinetic Parameters

References & Links

Literature References (3)

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Show Reference (3 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

650502

12843611

His151 and His296 are the acid-base catalytic residues of Bacillus cereus sphingomyelinase in sphingomyelin hydrolysis

2003

Obama, T.; Fujii, S.; Ikezawa, H.; Ikeda, K.; Imagawa, M.; Tsukamoto, K.

Biol. Pharm. Bull.

26

920-926

651801

12761162

Glu-53 of Bacillus cereus sphingomyelinase acts as an indispensable ligand of Mg2+ essential for catalytic activity

2003

Obama, T.; Kan, Y.; Ikezawa, H.; Imagawa, M.; Tsukamoto, K.

J. Biochem.

133

279-286

652444

12801930

Activation of human acid sphingomyelinase through modification or deletion of C-terminal cysteine

2003

Qiu, H.; Edmunds, T.; Baker-Malcolm, J.; Karey, K.P.; Estes, S.; Schwarz, C.; Hughes, H.; Van Patten, S.M.

J. Biol. Chem.

278

32744-32752

Links to other databases for 2-N-Hexadecanoylamino-4-nitrophenol

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Show Links (1 entry)

ChEBI

PubChem

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