Examples of 'glutamate dehydrogenase' in a sentence
Meaning of "glutamate dehydrogenase"
glutamate dehydrogenase: Glutamate dehydrogenase is an enzyme that plays a role in amino acid metabolism. It is involved in the conversion of glutamate to alpha-ketoglutarate and ammonia, impacting various physiological processes
How to use "glutamate dehydrogenase" in a sentence
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glutamate dehydrogenase
The glutamate dehydrogenase was fractionated to charge isomers.
The gdh gene coding for glutamate dehydrogenase.
Glutamate dehydrogenase in the kidney rose only in ammonium chloride treated animals.
The gdhA gene which codes for glutamate dehydrogenase.
Glutamate dehydrogenase is an enzyme responsible for ammonium assimilation and glutamate catabolism in organisms.
The assay is a kinetic assay with urease and glutamate dehydrogenase.
Glutamate dehydrogenase was purchased from Boeringer.
The basic and acidic charge isomers of glutamate dehydrogenase were not suppressed.
Glutamate dehydrogenase in the cheese-making process.
The enzyme apparently was soluble and could be separated from glutamate dehydrogenase and NADH oxidase.
Glutamate dehydrogenase catalyzes the reductive amination of α-ketoglutarate to glutamate.
In vertebrates, the activity of glutamate dehydrogenase is allosterically regulated.
In some embodiments, the substance of interest is glutamate dehydrogenase.
Glutamate can be deaminated by glutamate dehydrogenase or transaminated to form α-ketoglutarate.
Kinetic, enzymatic method with urease and glutamate dehydrogenase.
See also
No NADPH-dependent glutamate dehydrogenase activity could be detected in correct transformants.
This gene encodes an NAD-linked glutamate dehydrogenase.
However, glutamate dehydrogenase also plays a substantial facilitative role in glutamate 's metabolism.
Mitochondria did not seem to contain NAD-linked glutamate dehydrogenase.
The function of glutamate dehydrogenase was studied in cultured sweetpotato ( Ipomoea batatas ) nodal explants.
The glutamate produced is converted to 2-OG by a kinetic excess of glutamate dehydrogenase.
For example, glutamate dehydrogenase requires NADPH as a coenzyme in an L-glutamic acid biosynthetic pathway.
Corynebacterium glutamicum was transformed with a gene from Peptostreptococcus asaccharolyticus encoding an NAD-dependent glutamate dehydrogenase.
Some hospitals use a glutamate dehydrogenase ( GDH ) in conjuction with an EIA test.
The expressible enzyme activity ( a ) may be that of an NADH-dependent glutamate dehydrogenase.
These allow GLUD2-encoded glutamate dehydrogenase to work better in the brain than the GLUD1-encoded enzyme.
This is the origin of GLUD2, a retrogene derived from GLUD1, which encodes glutamate dehydrogenase.
Glutamate dehydrogenase ( GLDH ) catalyzes the following reaction,.
There are several cataplerotic enzymes ; these include PEPCK, aspartate aminotransferase, and glutamate dehydrogenase.
The roles of glutamate dehydrogenase ( GDH ) are postulated, as indicated by the dashed lines.
GDH-HI is caused by a mutation in the enzyme glutamate dehydrogenase ( GDH ).
Glutamate dehydrogenase was purchased from Boehringer Mannheim ( Roche diagnostics GmBH Mannheim, Germany ).
NADP-specific glutamate dehydrogenase.
SEQ ID NO, 22 is a nucleotide sequence encoding an NAD-dependent glutamate dehydrogenase.
Nissen et al ( 2000 ) disclose an approach in which the enzyme NADPH-dependent glutamate dehydrogenase was deleted.
SEQ ID NO, 21 is an amino acid sequence for an NAD-dependent glutamate dehydrogenase.
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Examples of using Glutamate
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Your glutamate levels are about the same
Riluzole is proposed to act by inhibiting glutamate processes
Glutamate is one of the neurotransmitters in the brain
Examples of using Dehydrogenase
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Increased lactate dehydrogenase level in your blood
Retinoid compounds are eliminated via alcohol dehydrogenase
An increase in lactate dehydrogenase is common but nonspecific
