5rla: Difference between revisions

Line 4:

==Overview==

Arginase is a thermostable (Tm = 75 degrees C) binuclear manganese, metalloenzyme which hydrolyzes l-arginine to form l-ornithine and urea., The three-dimensional structures of native metal-depleted arginase, metal-loaded H101N arginase, and metal-depleted H101N arginase have been, determined by X-ray crystallographic methods to probe the roles of the, manganese ion in site A (Mn2+A) and its ligand H101 in catalysis and, thermostability. We correlate these structures with thermal stability and, catalytic activity measurements reported here and elsewhere [Cavalli, R., C., Burke, C. J., Kawamoto, S., Soprano, D. R., and Ash, D. E. (1994), Biochemistry 33, 10652-10657]. We conclude that the substitution of a, wild-type histidine ligand to Mn2+A compromises metal binding, which in, turn compromises protein thermostability and catalytic function., Therefore, a fully occupied binuclear manganese metal cluster is required, for optimal catalysis and thermostability.

Arginase is a thermostable (Tm = 75 degrees C) binuclear manganese metalloenzyme which hydrolyzes l-arginine to form l-ornithine and urea. The three-dimensional structures of native metal-depleted arginase, metal-loaded H101N arginase, and metal-depleted H101N arginase have been determined by X-ray crystallographic methods to probe the roles of the manganese ion in site A (Mn2+A) and its ligand H101 in catalysis and thermostability. We correlate these structures with thermal stability and catalytic activity measurements reported here and elsewhere [Cavalli, R. C., Burke, C. J., Kawamoto, S., Soprano, D. R., and Ash, D. E. (1994) Biochemistry 33, 10652-10657]. We conclude that the substitution of a wild-type histidine ligand to Mn2+A compromises metal binding, which in turn compromises protein thermostability and catalytic function. Therefore, a fully occupied binuclear manganese metal cluster is required for optimal catalysis and thermostability.

==About this Structure==

Line 14:

[[Category: Rattus norvegicus]]

[[Category: Single protein]]

[[Category: Christianson, D.W.]]

[[Category: Christianson, D W.]]

[[Category: Kanyo, Z.F.]]

[[Category: Kanyo, Z F.]]

[[Category: Scolnick, L.R.]]

[[Category: Scolnick, L R.]]

[[Category: MN]]

[[Category: arginine metabolism]]

Line 22:

[[Category: urea cycle]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:53:35 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:49 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Arginase is a thermostable (Tm = 75 degrees C) binuclear manganese, metalloenzyme which hydrolyzes l-arginine to form l-ornithine and urea., The three-dimensional structures of native metal-depleted arginase, metal-loaded H101N arginase, and metal-depleted H101N arginase have been, determined by X-ray crystallographic methods to probe the roles of the, manganese ion in site A (Mn2+A) and its ligand H101 in catalysis and, thermostability. We correlate these structures with thermal stability and, catalytic activity measurements reported here and elsewhere [Cavalli, R., C., Burke, C. J., Kawamoto, S., Soprano, D. R., and Ash, D. E. (1994), Biochemistry 33, 10652-10657]. We conclude that the substitution of a, wild-type histidine ligand to Mn2+A compromises metal binding, which in, turn compromises protein thermostability and catalytic function., Therefore, a fully occupied binuclear manganese metal cluster is required, for optimal catalysis and thermostability.
+Arginase is a thermostable (Tm = 75 degrees C) binuclear manganese metalloenzyme which hydrolyzes l-arginine to form l-ornithine and urea. The three-dimensional structures of native metal-depleted arginase, metal-loaded H101N arginase, and metal-depleted H101N arginase have been determined by X-ray crystallographic methods to probe the roles of the manganese ion in site A (Mn2+A) and its ligand H101 in catalysis and thermostability. We correlate these structures with thermal stability and catalytic activity measurements reported here and elsewhere [Cavalli, R. C., Burke, C. J., Kawamoto, S., Soprano, D. R., and Ash, D. E. (1994) Biochemistry 33, 10652-10657]. We conclude that the substitution of a wild-type histidine ligand to Mn2+A compromises metal binding, which in turn compromises protein thermostability and catalytic function. Therefore, a fully occupied binuclear manganese metal cluster is required for optimal catalysis and thermostability.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Christianson, D.W.]]
+[[Category: Christianson, D W.]]
-[[Category: Kanyo, Z.F.]]
+[[Category: Kanyo, Z F.]]
-[[Category: Scolnick, L.R.]]
+[[Category: Scolnick, L R.]]
 [[Category: MN]]
 [[Category: arginine metabolism]]
@@ Line 22: / Line 22: @@
 [[Category: urea cycle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:53:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:49 2008''