Comment | This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2). |
References | RN [1]
RM PMID:10095071
RT Sequence and molecular analysis of the Rhizobium etli glsA gene, encoding a thermolabile glutaminase.
RA Calderon J, Huerta-Saquero A, Du Pont G, Duran S
RL Biochim Biophys Acta. 1999 Mar 19;1444(3):451-6.
RN [2]
RM PMID:18459799
RT Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis.
RA Brown G, Singer A, Proudfoot M, Skarina T, Kim Y, Chang C, Dementieva I, Kuznetsova E, Gonzalez CF, Joachimiak A, Savchenko A, Yakunin AF
RL Biochemistry. 2008 May 27;47(21):5724-35. |