Analysis of essential amino acid residues for catalytic activity of glutaminase from Micrococcus luteus K-3.
Structural-based mutational analysis of salt-tolerant glutaminase from Micrococcus luteus K-3 (Micrococcus glutaminase) revealed that three amino acid residues, S64, K67, and E160, were essential to a catalytic reaction. The result suggested that Micrococcus glutaminase had a possible catalytic mechanism similar to class A beta-lactamase rather than glutaminase-asparaginase from Pseudomonas 7A.
Yano
Shigekazu
S
Department of Bioscience and Bioengineering, Ritsumeikan University, 1-1-1 Noji-higashi, Kusatsu, Shiga 525-8577, Japan.
Kamemura
Aki
A
Yoshimune
Kazuaki
K
Moriguchi
Mitsuaki
M
Yamamoto
Sachiko
S
Tachiki
Takashi
T
Wakayama
Mamoru
M
D019943:Amino Acid Substitution; D000601:Amino Acids, Essential / Q000737:chemistry*; D001665:Binding Sites; D002384:Catalysis; D004789:Enzyme Activation; D005972:Glutaminase / Q000737:chemistry*; D016982:Micrococcus luteus / Q000201:enzymology*; D009154:Mutation; D011485:Protein Binding; D013329:Structure-Activity Relationship
D000601:Amino Acids, Essential; D005972:Glutaminase