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  2. Glyoxylate cycle - Wikipedia

    en.wikipedia.org/wiki/Glyoxylate_cycle

    The glyoxylate cycle, a variation of the tricarboxylic acid cycle, is an anabolic pathway occurring in plants, bacteria, protists, and fungi. The glyoxylate cycle centers on the conversion of acetyl-CoA to succinate for the synthesis of carbohydrates . [ 1 ]

  3. Glyoxylic acid - Wikipedia

    en.wikipedia.org/wiki/Glyoxylic_acid

    Glyoxylate is an intermediate of the glyoxylate cycle, which enables organisms, such as bacteria, [13] fungi, and plants [14] to convert fatty acids into carbohydrates. The glyoxylate cycle is also important for induction of plant defense mechanisms in response to fungi. [ 15 ]

  4. Glyoxylate and dicarboxylate metabolism - Wikipedia

    en.wikipedia.org/wiki/Glyoxylate_and_dicarboxyl...

    Glyoxylate and dicarboxylate metabolism describes a variety of reactions involving glyoxylate or dicarboxylates.Glyoxylate is the conjugate base of glyoxylic acid, and within a buffered environment of known pH such as the cell cytoplasm these terms can be used almost interchangeably, as the gain or loss of a hydrogen ion is all that distinguishes them, and this can occur in the aqueous ...

  5. Glyoxylate reductase - Wikipedia

    en.wikipedia.org/wiki/Glyoxylate_reductase

    Glyoxylate reductase (EC 1.1.1.26), first isolated from spinach leaves, [2] is an enzyme that catalyzes the reduction of glyoxylate to glycolate, using the cofactor NADH or NADPH. The systematic name of this enzyme class is glycolate:NAD + oxidoreductase .

  6. Isocitrate lyase - Wikipedia

    en.wikipedia.org/wiki/Isocitrate_lyase

    Isocitrate lyase (EC 4.1.3.1), or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. [2] [3] Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle (TCA cycle) and is used by bacteria, fungi, and plants.

  7. Malate synthase - Wikipedia

    en.wikipedia.org/wiki/Malate_synthase

    The glyoxylate shunt is essential for Pseudomonas aeruginosa growth in a host organism. In 2017, McVey, et al. examined the 3D structure of P. aeruginosa malate synthase G. They found that it is a monomer composed of four domains and is highly conserved in other pathogens.

  8. Glyoxysome - Wikipedia

    en.wikipedia.org/wiki/Glyoxysome

    Besides peroxisomal functions, glyoxysomes possess additionally the key enzymes of the glyoxylate cycle (isocitrate lyase and malate synthase) which accomplish the glyoxylate cycle bypass. [ 2 ] Thus, glyoxysomes (as all peroxisomes) contain enzymes that initiate the breakdown of fatty acids and additionally possess the enzymes to produce ...

  9. Glyoxylate reductase (NADP+) - Wikipedia

    en.wikipedia.org/wiki/Glyoxylate_reductase_(NADP+)

    In enzymology, a glyoxylate reductase (NADP +) (EC 1.1.1.79) is an enzyme that catalyzes the chemical reaction glycolate + NADP + ⇌ {\displaystyle \rightleftharpoons } glyoxylate + NADPH + H + Thus, the two substrates of this enzyme are glycolate and NADP + , whereas its 3 products are glyoxylate , NADPH , and H + .