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  2. Plasmepsin I - Wikipedia

    en.wikipedia.org/wiki/Plasmepsin_I

    Plasmepsin I (EC 3.4.23.38, aspartic hemoglobinase I, PFAPG, malaria aspartic hemoglobinase) is an enzyme. [1] [2] [3] This enzyme catalyses the following chemical reaction. Hydrolysis of the -Phe 33-Leu- bond in the alpha-chain of hemoglobin, leading to denaturation of the molecule. This enzyme is present in the malaria organism, Plasmodium.

  3. Cytochrome b5 reductase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_b5_reductase

    Oxidation and reduction pathways of methemoglobin and hemoglobin. Published by N. De Crem et al., 2022. In living organisms, because methemoglobin (MetHb) is unable to bind oxygen, it must be reduced to hemoglobin (Hb) through the action of the soluble isoform of cytochrome b5 reductase.

  4. Heme oxygenase - Wikipedia

    en.wikipedia.org/wiki/Heme_oxygenase

    HMOX1 is the rate-limiting step of heme catabolism that is dependent on NADPH-cytochrome P450 reductase and oxygen to cleave heme/porphyrin ring at the alpha-methene bridge to form biliverdin (or verdoglobin if the heme is still intact as hemoglobin). The reaction comprises three steps, which may be: [24] Heme b 3+ + O 2 + NADPH + H +

  5. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    In the first step, heme is converted to biliverdin by the enzyme heme oxygenase (HO). [36] NADPH is used as the reducing agent, molecular oxygen enters the reaction, carbon monoxide (CO) is produced and the iron is released from the molecule as the ferrous ion (Fe 2+ ). [ 37 ]

  6. Plasmepsin II - Wikipedia

    en.wikipedia.org/wiki/Plasmepsin_II

    Plasmepsin II (EC 3.4.23.39, aspartic hemoglobinase II, PFAPD) is an enzyme. [1] [2] [3] This enzyme catalyses the following chemical reaction. Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves the small molecule substrates such as Ala-Leu-Glu-Arg-Thr-Phe-Phe(NO 2)-Ser-Phe-Pro-Thr

  7. VHb (hemoglobin) - Wikipedia

    en.wikipedia.org/wiki/VHb_(hemoglobin)

    [29] [30] In these cases, increases in degradation are thought to be due both to the effects of VHb enhancing respiration to provide cells with additional ATP for growth and production of degrading enzymes, and delivery of oxygen directly to the oxygenases required for early steps in the degradative pathways.

  8. Luebering–Rapoport pathway - Wikipedia

    en.wikipedia.org/wiki/Luebering–Rapoport_pathway

    In biochemistry, the Luebering–Rapoport pathway (also called the Luebering–Rapoport shunt) is a metabolic pathway in mature erythrocytes involving the formation of 2,3-bisphosphoglycerate (2,3-BPG), which regulates oxygen release from hemoglobin and delivery to tissues. 2,3-BPG, the reaction product of the Luebering–Rapoport pathway was first described and isolated in 1925 by the ...

  9. Nucleic acid metabolism - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_metabolism

    Degradation of nucleic acids is a catabolic reaction and the resulting parts of the nucleotides or nucleobases can be salvaged to recreate new nucleotides. Both synthesis and degradation reactions require multiple enzymes to facilitate the event. Defects or deficiencies in these enzymes can lead to a variety of diseases. [1]