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  2. Zn2+-exporting ATPase - Wikipedia

    en.wikipedia.org/wiki/Zn2+-exporting_ATPase

    The 3 substrates of this enzyme are ATP, H 2 O, and Zn 2+, whereas its 3 products are ADP, phosphate, and Zn 2+. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Zn 2+-exporting).

  3. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...

  4. Enzyme Commission number - Wikipedia

    en.wikipedia.org/wiki/Enzyme_Commission_number

    The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. [1] As a system of enzyme nomenclature, every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions.

  5. Glycine N-acyltransferase - Wikipedia

    en.wikipedia.org/wiki/Glycine_N-acyltransferase

    Thus, the two substrates of this enzyme are acyl-CoA and glycine, whereas its two products are CoA and N-acylglycine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:glycine N-acyltransferase. Other names ...

  6. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. [67] The rate data used in kinetic analyses are commonly obtained from enzyme assays . In 1913 Leonor Michaelis and Maud Leonora Menten proposed a quantitative theory of enzyme kinetics, which is referred to as Michaelis–Menten kinetics . [ 68 ]

  7. Hydroperoxide dehydratase - Wikipedia

    en.wikipedia.org/wiki/Hydroperoxide_dehydratase

    The systematic name of this enzyme class is (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]. Other names in common use include hydroperoxide isomerase , linoleate hydroperoxide isomerase , linoleic acid hydroperoxide isomerase , HPI , (9 Z ,11 E ,14 Z )-(13 S ...

  8. Deoxyribose-phosphate aldolase - Wikipedia

    en.wikipedia.org/wiki/Deoxyribose-phosphate_aldolase

    The systematic name of this enzyme class is 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase (D-glyceraldehyde-3-phosphate-forming). Other names in common use include phosphodeoxyriboaldolase , deoxyriboaldolase , deoxyribose-5-phosphate aldolase , 2-deoxyribose-5-phosphate aldolase , and 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase .

  9. Phosphate acetyltransferase - Wikipedia

    en.wikipedia.org/wiki/Phosphate_acetyltransferase

    The substrates of this enzyme are acetyl-CoA and phosphate, whereas its two products are CoA and acetyl phosphate. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:phosphate acetyltransferase.