Glutamine formation Glutamine synthetase catalyzes the following reaction Glutamate NH3 ATP Glutamine ADP Pi

The E. coli glutamine synthetase is a dodecamer, with 12 identical subunits and the complex has a molecular weight of about 600,000 Daltons. The amide nitrogen of glutamate is used for the synthesis of several amino acids, purine and pyrimidine nucleotides, and amino sugars, so glutamine synthetase plays a central role in nitrogen metabolism. In animals, the enzyme is a key participant in detoxifying ammonia, particularly in the brain, and in ammonia excretion in the kidney. Accumulation of glutamate and glutamine depletes oi-ketoglutarate, which would interfere with the citric acid cycle. As a result, glutamine synthetase tightly regulated. Mechanisms include the following:

Cumulative feedback Inhibition - Eight specific feedback inhibitors, which are either metabolic end products of glutamine (tryptophan, histidine, glucosamine-6-phosphate, carbamoyl phosphate, CTP, or AMP) or indicators of the general status of amino acid metabolism (alanine or glycine), can bind to any of the subunits of the enzyme and at least partially inhibit it. The more inhibitors that bind, the greater the inhibition.

Covalent modification (adenylylation) - A specific tyrosine residue in glutamine synthetase can react with ATP to form a phosphate ester with AMP (see here). Adenylylation renders the catalytic site of the enzyme inactive. Adenylylation and deadenylylation involve a complex series of regulatory cascades. Figure 20.9 shows regulatory mechanisms of the E. coli enzyme. Both processes are catalyzed by the same enzyme-a complex of adenylyl transferase (AT) and a regulatory protein, PII. The form of PII determines whether the AT-PII complex catalyzes adenylylation or deadenylylation. If PII is uridylyated, the AT-PII complex catalyzes deadenylylation. Deuridylylation of PII causes the AT-PII complex to catalyze adenylylation. The enzyme uridylyl transferase catalyzes uridylylation of PII, whereas deuridylylation is catalyzed by a different enzyme. Uridylyl transferase is allosterically regulated, with ATP and ot-ketoglutarate activating it and glutamine inhibits it.

Asparagine formation - Asparagine synthetase catalyzes the conversion of aspartate to asparagine as follows:

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  • aira
    What is the enzyme that catalyze glutamate nh3?
    6 years ago

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