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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.
This process transfers the amino group instead of losing the amino group to be converted into ammonium. The amino group is transferred to α-ketoglutarate, so that it can be converted to glutamate. Then glutamate transfers the amino group to oxaloacetate. This transfer is so that the oxaloacetate can be converted to aspartate or other amino acids.
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 ...
The high Km of GLUT2 allows for glucose sensing; rate of glucose entry is proportional to blood glucose levels. GLUT4 transporters are insulin sensitive, and are found in muscle and adipose tissue. As muscle is a principal storage site for glucose and adipose tissue for triglyceride (into which glucose can be converted for storage), GLUT4 is ...
[24] For example, methylamine:L-glutamate N-methyltransferase would be the standard naming convention for the transferase methylamine-glutamate N-methyltransferase, where methylamine is the donor, L-glutamate is the acceptor, and methyltransferase is the EC category grouping. This same action by the transferase can be illustrated as follows:
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Alanine transaminase (ALT), also known as alanine aminotransferase (ALT or ALAT), formerly serum glutamate-pyruvate transaminase (GPT) or serum glutamic-pyruvic transaminase (SGPT), is a transaminase enzyme (EC 2.6.1.2) that was first characterized in the mid-1950s by Arthur Karmen and colleagues. [1]