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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.
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.
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.
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.
Consequently, during exercise when the ATP reservoir is low (ADP>ATP), glutamate is produced from branch-chained amino acids (BCAAs) and α-ketoglutarate, as well as from alanine and α-ketoglutarate. [12] Glutamate is then used to produce aspartate. The aspartate enters the purine nucleotide cycle, where it is used to convert IMP into S-AMP ...
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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
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