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  2. Isozyme - Wikipedia

    en.wikipedia.org/wiki/Isozyme

    In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different K M values), or are regulated differently.

  3. Enolase - Wikipedia

    en.wikipedia.org/wiki/Enolase

    Enolase is a member of the large enolase superfamily.It has a molecular weight of 82,000–100,000 daltons depending on the isoform. [3] [4] In human alpha enolase, the two subunits are antiparallel in orientation so that Glu 20 of one subunit forms an ionic bond with Arg 414 of the other subunit. [3]

  4. Alpha-enolase - Wikipedia

    en.wikipedia.org/wiki/Alpha-enolase

    Enolase 1 (ENO1), more commonly known as alpha-enolase, is a glycolytic enzyme expressed in most tissues, one of the isozymes of enolase.Each isoenzyme is a homodimer composed of 2 alpha, 2 gamma, or 2 beta subunits, and functions as a glycolytic enzyme.

  5. Hexokinase - Wikipedia

    en.wikipedia.org/wiki/Hexokinase

    Hexokinase II/B constitutes the principal regulated isoenzyme in many cell types and is increased in many cancers. It is the hexokinase found in muscle and heart. Hexokinase II is also located at the mitochondria outer membrane so it can have direct access to ATP. [ 7 ]

  6. Isoenzymes - Wikipedia

    en.wikipedia.org/?title=Isoenzymes&redirect=no

    Download QR code; Print/export Download as PDF; Printable version; In other projects ... From Wikipedia, the free encyclopedia. Redirect page. Redirect to: Isozyme ...

  7. Aldolase B - Wikipedia

    en.wikipedia.org/wiki/Aldolase_B

    Aldolase B is a homotetrameric enzyme, composed of four subunits with molecular weights of 36 kDa with local 222 symmetry. Each subunit has a molecular weight of 36 kDa and contains an eight-stranded α/β barrel, which encloses lysine 229 (the Schiff-base forming amino acid that is key for catalysis).

  8. Isocitrate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Isocitrate_dehydrogenase

    The overall free energy for this reaction is -8.4 kJ/mol. [12] Catalytic mechanism of the breakdown of isocitrate into oxalosuccinate, then into a final product of alpha-ketoglutarate. The oxalosuccinate intermediate is hypothetical; it has never been observed in the decarboxylating version of the enzyme.

  9. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different molecules by differences in their isoelectric point (pI). [ 1 ] [ 2 ] It is a type of zone electrophoresis usually performed on proteins in a gel that takes advantage of the fact that overall charge on the molecule of interest is a function of the ...

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