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  2. Glycolysis - Wikipedia

    en.wikipedia.org/wiki/Glycolysis

    d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...

  3. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    This article needs attention from an expert in biochemistry.The specific problem is: someone with a solid grasp of the full scope of this subject and of its secondary and advanced teaching literatures needs to address A, the clear structural issues of the article (e.g., general absence of catabolic biosynthetic pathways, insertion of macromolecule anabolic paths before all building blocks ...

  4. 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.

  5. Oligopeptidase - Wikipedia

    en.wikipedia.org/wiki/Oligopeptidase

    The history of oligopeptidases originates in the late 1960s, when the rabbit brain was searched for enzymes that cause inactivation of the nonapeptide bradykinin. [5] In the early and mid 1970s two thiol-activated endopeptidases, responsible for more than 90% of bradykinin inactivation, were isolated from cytosol of rabbit brain, and characterized.

  6. Aminoacylase - Wikipedia

    en.wikipedia.org/wiki/Aminoacylase

    In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction. N-acyl-L-amino acid + H 2 O ⇌ carboxylate + L-amino acid. Thus, the two substrates of this enzyme are N-acyl-L-amino acid and H 2 O, whereas its two products are carboxylate and L-amino acid.

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Since most enzymes have an optimum pH of 6 to 7, the amino acids in the side chain usually have a pK a of 4~10. Candidate include aspartate, glutamate, histidine, cysteine. These acids and bases can stabilise the nucleophile or electrophile formed during the catalysis by providing positive and negative charges. [6]: 164–70

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  9. Phosphofructokinase 1 - Wikipedia

    en.wikipedia.org/wiki/Phosphofructokinase_1

    Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors. PFK-1 catalyzes the important "committed" step of glycolysis, the conversion of fructose 6-phosphate and ATP to fructose 1,6-bisphosphate and ...

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