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・ Glutamate-1-semialdehyde
・ Glutamate-1-semialdehyde 2,1-aminomutase
・ Glutamate-5-semialdehyde
・ Glutamate-5-semialdehyde dehydrogenase
・ Glutamate-glutamine cycle
・ Glutamatergic
・ Glutamate–cysteine ligase
・ Glutamate—ethylamine ligase
・ Glutamate—methylamine ligase
・ Glutamate—prephenate aminotransferase
・ Glutamate—putrescine ligase
・ Glutamate—tRNA ligase
・ Glutamate—tRNA(Gln) ligase
・ Glutamic acid
・ Glutamic acid (data page)
Glutamic protease
・ Glutamin-(asparagin-)ase
・ Glutaminase
・ Glutamine
・ Glutamine (data page)
・ Glutamine amidotransferase
・ Glutamine N-acyltransferase
・ Glutamine N-phenylacetyltransferase
・ Glutamine oxoglutarate aminotransferase
・ Glutamine synthetase
・ Glutamine—fructose-6-phosphate transaminase (isomerizing)
・ Glutamine—phenylpyruvate transaminase
・ Glutamine—pyruvate transaminase
・ Glutamine—scyllo-inositol transaminase
・ Glutamine—tRNA ligase


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Glutamic protease : ウィキペディア英語版
Glutamic protease

Glutamic proteases are a group of proteolytic enzymes containing a glutamic acid residue within the active site. This type of protease was first described in 2004 and became the sixth catalytic type of protease. Members of this group of protease had been previously assumed to be an aspartate protease, but structural determination showed it to belong to a novel protease family. The first structure of this group of protease was scytalidoglutamic peptidase, the active site of which contains a catalytic dyad, glutamic acid (E) and glutamine (Q), which give rise to the name eqolisin. This group of proteases are found primarily in pathogenic fungi affecting plant and human.〔
==Distribution and types==
This group of proteases have a limited distribution, and were originally thought to be limited to filamentous fungi mainly in the Ascomycota phylum. Subsequently, however, glutamic proteases have been identified in bacteria and archaea.
These proteases were first identified in the fungi ''Scytalidium lignicola'' and ''Aspergillus niger var. macrosporus'', from which scytalidoglutamic peptidase (eqolisin) and aspergilloglutamic peptidase are derived respectively. These two proteases contain active site Glu and Gln residues and are grouped under MEROPS family G1.
A convergently evolved glutamic peptidase, the pre-neck appendage protein (bacteriophage phi-29), uses a Glu and an Asp residue at the active site, and is classified as MEROPS family G2.〔(【引用サイトリンク】title=Family G2 )

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