: glutamate and glutamine metabolism

: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Metabolic pathways

: L-glutamate biosynthesis I,
L-asparagine biosynthesis III (tRNA-dependent),
glutaminyl-tRNAgln biosynthesis via transamidation,
ammonia assimilation cycle III,
L-citrulline biosynthesis,
L-glutamine degradation I

: BR22683

: R00256

: GLUTAMIN-RXN, RXN-22710

: 762

: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)

: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.

: glutamate and glutamine metabolism

: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Metabolic pathways

: L-glutamate biosynthesis I,
L-asparagine biosynthesis III (tRNA-dependent),
glutaminyl-tRNAgln biosynthesis via transamidation,
ammonia assimilation cycle III,
L-citrulline biosynthesis,
L-glutamine degradation I

: BR22683

: R00256

: GLUTAMIN-RXN, RXN-22710

: 762

: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)

: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.

: glutamate and glutamine metabolism

: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Metabolic pathways

: L-glutamate biosynthesis I,
L-asparagine biosynthesis III (tRNA-dependent),
glutaminyl-tRNAgln biosynthesis via transamidation,
ammonia assimilation cycle III,
L-citrulline biosynthesis,
L-glutamine degradation I

: BR22683

: R00256

: GLUTAMIN-RXN, RXN-22710

: 762

: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)

: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.

: glutamate and glutamine metabolism

: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Metabolic pathways

: L-glutamate biosynthesis I,
L-asparagine biosynthesis III (tRNA-dependent),
glutaminyl-tRNAgln biosynthesis via transamidation,
ammonia assimilation cycle III,
L-citrulline biosynthesis,
L-glutamine degradation I

: BR22683

: R00256

: GLUTAMIN-RXN, RXN-22710

: 762

: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)

: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.

: glutamate and glutamine metabolism

: Arginine biosynthesis,
Alanine, aspartate and glutamate metabolism,
Metabolic pathways

: L-glutamate biosynthesis I,
L-asparagine biosynthesis III (tRNA-dependent),
glutaminyl-tRNAgln biosynthesis via transamidation,
ammonia assimilation cycle III,
L-citrulline biosynthesis,
L-glutamine degradation I

: BR22683

: R00256

: GLUTAMIN-RXN, RXN-22710

: 762

: ec 2.6.1.85 (see R01716, R00256+R05552) ec 6.3.4.2 (see R00573, R00256+R00571) ec 6.3.5.4 (see R00578, R00256+R00483) ec 6.3.5.5 (see R00575, R00256+R10948+R10949+R01395) ec 2.6.1.123 (see R12939, R00256+R12937+R12938)

: Glutaminase hydrolyzes GLN, releasing AMMONIA. When the glutaminase is a free-standing enzyme, the released ammonia quickly binds a proton to become |FRAME:AMMONIUM|, which is more stable at neutral pH. However, many enzymes are multifunctional, containing both a glutaminase domain and an additional domain that utilizes ammonia. The two active sites in such enzymes are connected by channel through which the ammonia molecules are transferred directly to the next active site. These channels are specific for AMMONIA and do not transfer AMMONIUM ions |CITS: [Mullins99][15849257][17559838][18220365][19921932]|. This is different from stand-alone glutaminases, which can produce ammonium, the more stable form under neutral pH.