Comparison of the properties of histidine ammonia-lyase in normal and histidinemic mutant mice.
The histidinemic (his/his) mutant mouse shows greatly reduced skin and liver histidine:ammonia-lyase (HAL; EC 4.3.1.3) activity compared with normal mice. Liver HAL activity in the mutant is heat and salt labile and is inhibited at high substrate concentrations. Two HAL components have been identified in the normal mouse liver, a minor component with properties similar to those of HAL of the mutant mouse and a major component which is heat and salt stable and insensitive to substrate inhibition. Immunotitration with anti-HAL antibody shows that the livers of mutant mice contain no detectable antigenically cross-reacting HAL protein. It is concluded, therefore, that the his allele is a null allele at a structural or regulatory locus for the major HAL enzyme and maps close to the HAL-regulatory locus Hsd and that te low residual HAL activity in the mutant is due to another enzyme.
D000483:Alleles; D000642:Ammonia-Lyases / Q000378:metabolism*; D000818:Animals; D008040:Genetic Linkage; D006639:Histidine / Q000378:metabolism*; D006638:Histidine Ammonia-Lyase / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D051379:Mice / Q000235:genetics*; D009154:Mutation; D009994:Osmolar Concentration
D007527:Isoenzymes; D006639:Histidine; D000642:Ammonia-Lyases; D006638:Histidine Ammonia-Lyase