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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. Glucose-1,6-bisphosphate synthase - Wikipedia

    en.wikipedia.org/wiki/Glucose-1,6-bisphosphate...

    The main product, glucose-1,6-bisphosphate, appears to have several functions: 1. Inhibition of hexokinase, an enzyme used in the first step of glycolysis. [2]2. Activation of phosphofructokinase-1 (PFK-1) and pyruvate kinase, both of which are enzymes involved in activation of the glycolyt

  4. Glycosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Glycosyltransferase

    Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...

  5. Phosphoglycerate kinase - Wikipedia

    en.wikipedia.org/wiki/Phosphoglycerate_kinase

    PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG. In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2.

  6. Transferase - Wikipedia

    en.wikipedia.org/wiki/Transferase

    In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor). [2] They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life ...

  7. Triosephosphate isomerase - Wikipedia

    en.wikipedia.org/wiki/Triosephosphate_isomerase

    This structural motif is called an αβ-barrel, or a TIM-barrel, and is by far the most commonly observed protein fold. The active site of this enzyme is in the center of the barrel. A glutamic acid residue and a histidine are involved in the catalytic mechanism. The sequence around the active site residues is conserved in all known triose ...

  8. Carbohydrate metabolism - Wikipedia

    en.wikipedia.org/wiki/Carbohydrate_metabolism

    Glucose regulation and product use are the primary categories in which these pathways differ between organisms. [2] In some tissues and organisms, glycolysis is the sole method of energy production. [2] This pathway is common to both anaerobic and aerobic respiration. [1] Glycolysis consists of ten steps, split into two phases. [2]

  9. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    The process is non-templated (unlike DNA transcription or protein translation); instead, the cell relies on segregating enzymes into different cellular compartments (e.g., endoplasmic reticulum, cisternae in Golgi apparatus). Therefore, glycosylation is a site-specific modification.

  1. Related searches enzyme involved in glycolysis is called the main product of translation

    glycosyltransferase enzymesglycosyltransferase a and b