Abstract: Glutamine aminohydrolase (glutaminase or l-glutaminase; EC 3.5.1.2) is an amidase enzyme that converts glutamine to glutamate with the release of ammonia. It acts as an endopeptidase, hydrolyzing the peptide bonds present in the interior of a protein molecule [1]. The enzyme was named after the discovery of its activity by Hans Krebs in 1935. It mainly catalyzes the hydrolysis of the γ-amido bond of l-glutamine and it plays a major role in the nitrogen metabolism of both prokaryotes and eukaryotes [2]. Glutaminase is seen in the inner membrane of mitochondria and is the predominant glutamine-using enzyme in the brain. Microorganisms are also well known producers of this commercially important enzyme. l-Glutaminase is widely used as an oncolytic enzyme and as an antiretroviral agent because of its capability to degrade small molecules like glutamine. Glutaminase also finds application in the food industry as a flavor-enhancing agent. The sources, production strategies, characteristics, and applications of l-glutaminase are discussed here.
Publication Year: 2016
Publication Date: 2016-09-24
Language: en
Type: book-chapter
Indexed In: ['crossref']
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Cited By Count: 7
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