caa a22 4500 475846540 CHVBK 20180406123915.0 cr unu---uuuuu 170329e20001001xx s 000 0 eng 10.1007/PL00000646 doi (NATIONALLICENCE)springer-10.1007/PL00000646 Intragenic complementation and the structure and function of argininosuccinate lyase [Elektronische Daten] [B. Yu, P. L. Howell] Abstract.: Argininosuccinate lyase (ASL) catalyzes the reversible hydrolysis of argininosuccinate to arginine and fumarate, a reaction important for the detoxification of ammonia via the urea cycle and for arginine biosynthesis. ASL belongs to a superfamily of structurally related enzymes, all of which function as tetramers and catalyze similar reactions in which fumarate is one of the products. Genetic defects in the ASL gene result in the autosomal recessive disorder argininosuccinic aciduria. This disorder has considerable clinical and genetic heterogeneity and also exhibits extensive intragenic complementation. Intragenic complementation is a phenomenon that occurs when a multimeric protein is formed from subunits produced by different mutant alleles of a gene. The resulting hybrid protein exhibits greater enzymatic activity than is found in either of the homomeric mutant proteins. This review describes the structure and function of ASL and its homologue δ crystallin, the genetic defects associated with argininosuccinic aciduria and current theories regarding complementation in this protein. Birkhäuser Verlag Basel,, 2000 Key words. Argininosuccinate lyase nationallicence delta crystallin nationallicence argininosuccinic aciduria nationallicence intragenic complementation nationallicence Yu B. Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, M5S 1A8, Ontario (Canada), CA aut Howell P. L. Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, M5S 1A8, Ontario (Canada), CA aut https://doi.org/10.1007/PL00000646 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/PL00000646 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Yu B. Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, M5S 1A8, Ontario (Canada), CA aut NATIONALLICENCE 700 1- Howell P. L. Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, M5S 1A8, Ontario (Canada), CA aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer