Glutamine formula

This enzyme catalyzes the hydrolysis of glutamine (Formula 2.113). For meat preparations, the addition of an enzyme preparation from Bacillus subtilis is under discussion. It increases the concentration of glutamic acid, which substantially contributes to the taste of meat. 

Glutamine (Gin or Q) ((2S )-2-amino-4-carbamoyl-butanoic acid) is a polar, uncharged amino acid with the formula HOOCCH(NH2)(CH2)2CONH2. The abbreviation Glx or Z represents either Gin or Glu. The side chain contains an amide group in place of the carboxylate and can be considered the amide of the acidic amino acid Glu. Gin is the most abundant naturally occurring, nonessential amino acid in the human body. It becomes conditionally essential in states of illness or injury. Both glutamate and Gin play key roles in nitrogen metabolism. ... 

Considering the influence of media components on specific production rate, only one expression makes serum relevant (Equation 69), while glutamine appears as a limiting substrate in three formulas (Equations 69 to 71), always with a Monod-type structure. Glucose shows either an inhibitory effect over production (Equations 71 and 72), or a limiting and inhibitory pattern simultaneously (Equations 70). Instead of the classical... 

The other product of the reaction is 4-(3-0-phospho-D-erj/fftro-trihy-droxypropyl)imidazole (XXXIII). In the absence of glutamine, an intermediate is detectable. Formula XXXIV is suggested for this substance. 

An overwhelming majority of foods contain AA, either in the free form (e.g., fruit juice) or in the form of protein (partially hydrolyzed or intact). Proteins are polymers of AA, and as such, represent the principal source of dietary AA for humans when enzymatically digested to liberate their constituents A A. Consequently, the determination of the AA content in food is important in a number of applications that include food as the sole source of nutrition (e.g., infant formula), prescribed fortified nutritional products (e.g., product enriched with glutamine), the verification of the absence of an specific AA in certain inborn errors of metabolism (e.g., phenylalaline in phenylketoneurea), as well as for regulatory concerns. 

Protein glutamine-y-glutamyl transferase (transglutaminase, TGase) catalyzes the acyl transfer between the y-carboxyamide group of peptide-bound glutamine (acyl donor) and primary amines (acyl acceptor, I in Formula 2.114), e. g., peptide-bound lysine (II in Formula 2.114). Free... 

Anthranilic acid (or o-amino-benzoic acid) is an aromatic acid with the formula C H NO, which consists of a substituted benzene ring with two adjacent, or "ortho- functional groups, a carboxylic acid, and an amine (Fig. 14.1). Anthranilic acid is biosynthesized from shikimic acid (for shikimic acid biosynthesis, see Chapter 10) following the chorismic acid-mediated pathway [1]. Based on its biosynthetic mechanism, shikimate is transformed to shikimate 3-phosphate with the consumption of one molecule of ATP, catalyzed by shikimate kinase. 5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase is then catalyze the addition of phosphoenolpyruvate to 3-phospho-shikimate followed by the elimination of phosphate, which leads to EPSP. EPSP is further transformed into chorismate by chorismate synthase. Chorismate reacts with glutamine to afford the final product anthranilate and glutamate pyruvate catalyzed by anthranilate synthase (Fig. 14.1). 

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