Glutamate synthase (also known as Glutamine oxoglutarate aminotransferase) is an
enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products ...
and frequently abbreviated as GOGAT. This enzyme manufactures
glutamate from
glutamine
Glutamine (symbol Gln or Q) is an α-amino acid that is used in the biosynthesis of proteins. Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide. It is classified as a charge-neutral ...
and
α-ketoglutarate, and thus along with
glutamine synthetase
Glutamine synthetase (GS) () is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine:
Glutamate + ATP + NH3 → Glutamine + ADP + phosphate
Glutam ...
(abbreviated GS) plays a central role in the regulation of
nitrogen
Nitrogen is the chemical element with the symbol N and atomic number 7. Nitrogen is a nonmetal and the lightest member of group 15 of the periodic table, often called the pnictogens. It is a common element in the universe, estimated at se ...
assimilation in photosynthetic eukaryotes and prokaryotes.
["Phylogenetic Relationships Among Glutamate Synthase (GOGAT) Enzymes" Eva Zadykowicz and Deborah L. Robertson; Department of Biology, Clark University, Worcester, MA]["Practical Streptomyces Genetics" Keiser et al; John Innes Foundation, Norwich, England] This is of great importance as primary productivity in many marine environments is regulated by the availability of inorganic nitrogen.
The primary sources of inorganic nitrogen used by marine algae are
nitrate and
ammonium. Both forms are ultimately incorporated into amino acids through the sequential reaction of glutamine synthetase (GS) and glutamate synthase (glutamine:2-oxoglutarate aminotransferase; GOGAT). GOGAT isoenzymes catalyze the transfer of the amido nitrogen of glutamine to 2-oxoglutarate using pyridine nucleotides (
NADH
Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an aden ...
-/
NADPH-dependent) or
ferredoxin (ferredoxin dependent) as reductants.
They are called
NADH-GOGAT and
Fd-GOGAT respectively. In photosynthetic eukaryotes, GS and GOGAT isoenzymes are localized in the
cytosol
The cytosol, also known as cytoplasmic matrix or groundplasm, is one of the liquids found inside cells ( intracellular fluid (ICF)). It is separated into compartments by membranes. For example, the mitochondrial matrix separates the mitochondri ...
and
chloroplast.
Fd-GOGAT is found strictly in
cyanobacteria and photosynthetic eukaryotes, and the gene is located in the chloroplast of
rhodophytes
Red algae, or Rhodophyta (, ; ), are one of the oldest groups of eukaryotic algae. The Rhodophyta also comprises one of the largest phyla of algae, containing over 7,000 currently recognized species with taxonomic revisions ongoing. The majority ...
and in the nucleus of vascular plants, but in both cases its product is active in the chloroplast. NADH-GOGAT is found in the nucleus of vascular plants, fungi, and diatoms, while NADPH-GOGAT is found in non-photosynthetic bacteria and
archaea.
See also
*
Glutamate synthase (NADPH)
In enzymology, a glutamate synthase (NADPH) () is an enzyme that catalyzes the chemical reaction
:L-glutamine + 2-oxoglutarate + NADPH + H+ \rightleftharpoons 2 L-glutamate + NADP+
Thus, the four substrates of this enzyme are L-glutamine, 2- ...
*
Glutamate synthase (NADH)
*
Glutamate synthase (ferredoxin)
References
{{DEFAULTSORT:Glutamine Oxoglutarate Aminotransferase
Enzymes