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  2. 5-oxoprolinase (ATP-hydrolysing) - Wikipedia

    en.wikipedia.org/wiki/5-oxoprolinase_(ATP...

    In enzymology, a 5-oxoprolinase (ATP-hydrolysing) (EC 3.5.2.9) is an enzyme that catalyzes the chemical reaction. ATP + 5-oxo-L-proline + 2 H 2 O ADP + phosphate + L-glutamate. The 3 substrates of this enzyme are ATP, 5-oxo-L-proline, and H 2 O, whereas its 3 products are ADP, phosphate, and L-glutamate.

  3. Pyroglutamic acid - Wikipedia

    en.wikipedia.org/wiki/Pyroglutamic_acid

    The names of pyroglutamic acid conjugate base, anion, salts, and esters are pyroglutamate, 5-oxoprolinate, or pidolate. Formation of pyroglutamic acid from N-terminal glutamine. It is a metabolite in the glutathione cycle that is converted to glutamate by 5-oxoprolinase. Pyroglutamate is found in many proteins including bacteriorhodopsin.

  4. Glutaminolysis - Wikipedia

    en.wikipedia.org/wiki/Glutaminolysis

    The conversion of the amino acid glutamine to α-ketoglutarate takes place in two reaction steps: Conversion of glutamine to α-ketoglutarate. 1. Hydrolysis of the amino group of glutamine yielding glutamate and ammonium. Catalyzing enzyme: glutaminase (EC 3.5.1.2) 2. Glutamate can be excreted or can be further metabolized to α-ketoglutarate.

  5. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.

  6. Glutaminase - Wikipedia

    en.wikipedia.org/wiki/Glutaminase

    Glutaminase (EC 3.5.1.2, glutaminase I, L-glutaminase, glutamine aminohydrolase) is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Glutaminase catalyzes the following reaction: Glutamine + H 2 O → glutamate + NH + 4

  7. Transaminase - Wikipedia

    en.wikipedia.org/wiki/Transaminase

    Animals must metabolize proteins to amino acids, at the expense of muscle tissue, when blood sugar is low. The preference of liver transaminases for oxaloacetate or alpha-ketoglutarate plays a key role in funneling nitrogen from amino acid metabolism to aspartate and glutamate for conversion to urea for excretion of nitrogen.

  8. Food poisoning is extremely common. But that doesn't ... - AOL

    www.aol.com/food-poisoning-extremely-common...

    Few things will put a damper on your vacation or holiday faster than food poisoning.The intense stomach pain, rushing to the toilet and feeling relegated to bed keeps just about everyone out of ...

  9. Glutamine synthetase - Wikipedia

    en.wikipedia.org/wiki/Glutamine_synthetase

    Glutamate + ATP + NH 3 → Glutamine + ADP + phosphate Glutamine synthetase catalyzed reaction. Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. [4] The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. [5] Other reactions may take ...