Structural highlights
FunctionGPUA_PSEAE Catalyzes the hydrolysis of 3-guanidinopropanoate to beta-alanine and urea. Possesses low activity against 4-guanidinobutanoate. Has no activity against arginine and agmatine.[1] Publication Abstract from PubMedPseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA) catalyze the hydrolysis of 4-guanidinobutyrate and 3-guanidinopropionate, respectively. They belong to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase. In this study, we have determined the crystal structures of GbuA and GpuA from P. aeruginosa to provide a structural insight into their substrate specificity. Although GbuA and GpuA share a common structural fold of the typical ureohydrolase superfamily, they exhibit significant variations in two active site loops. Mutagenesis of Met161 of GbuA and Tyr157 of GpuA, both of which are located in the active site loop 1 and predicted to be involved in substrate recognition, significantly affected their enzymatic properties, implying their important roles in catalysis. Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily.,Lee SJ, Kim DJ, Kim HS, Lee BI, Yoon HJ, Yoon JY, Kim KH, Jang JY, Im HN, An DR, Song JS, Kim HJ, Suh SW J Struct Biol. 2011 May 12. PMID:21600989[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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