title: Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily.
abstract: Pseudomonas 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.
authors: Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Republic of Korea.
authors: Sang Jae
authors: SJ
authors: Lee
authors: Do Jin
authors: DJ
authors: Kim
authors: Hyoun Sook
authors: HS
authors: Kim
authors: Byung Il
authors: BI
authors: Lee
authors: Hye-Jin
authors: HJ
authors: Yoon
authors: Ji Young
authors: JY
authors: Yoon
authors: Kyoung Hoon
authors: KH
authors: Kim
authors: Jun Young
authors: JY
authors: Jang
authors: Ha Na
authors: HN
authors: Im
authors: Doo Ri
authors: DR
authors: An
authors: Jin-Su
authors: JS
authors: Song
authors: Hie-Joon
authors: HJ
authors: Kim
authors: Se Won
authors: SW
authors: Suh