Literature summary for 6.3.1.2 extracted from

Jezek, M.; Geilfus, C.M.; Muehling, K.H.
Glutamine synthetase activity in leaves of Zea mays L. as influenced by magnesium status (2015), Planta, 242, 1309-1319 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required, Mg2+ is an integral component of the enzyme glutamine synthetase having both a structural and a catalytic role. Mg2+ is relevant for the posttranslational regulation of the enzyme	Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-glutamate + NH3	Zea mays	-	ADP + phosphate + L-glutamine	-	?

Organism

Organism	UniProt	Comment	Textmining
Zea mays	-	cv. Susann	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	GS activity is analyzed dependent on different leaf developmental stages, with or without Mg2+ starvation, overview	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamate + NH3	-	Zea mays	ADP + phosphate + L-glutamine	-	?

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Zea mays

General Information

General Information	Comment	Organism
malfunction	the total capacity of the enzyme-mediated ligation of free ammonium and glutamate to form glutamine in the leaves of maize plants is not impaired upon severe magnesium starvation. The total GS-mediated primary or secondary assimilation of free NH4+ is not a limiting enzymatic reaction under Mg-deficiency and thus cannot be accountable for the observed restriction of plant growth and productivity in Mg-deficient maize, phenotype, overview	Zea mays
physiological function	glutamine synthetase is one of the key enzymes in nitrogen assimilation, ligating-free ammonium to glutamate to form glutamine and it is therefore crucial for plant growth and productivity	Zea mays

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Release 2023.1 (January 2023)