Evidence for an inhibitory LIM domain in a rat brain agmatinase-like protein |
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Authors: | Castro Víctor Fuentealba Pablo Henríquez Adolfo Vallejos Alejandro Benítez José Lobos Marcela Díaz Beatriz Carvajal Nelson Uribe Elena |
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Affiliation: | Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción, Chile |
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Abstract: | We recently cloned a rat brain agmatinase-like protein (ALP) whose amino acid sequence greatly differs from other agmatinases and exhibits a LIM-like domain close to its carboxyl terminus. The protein was immunohistochemically detected in the hypothalamic region and hippocampal astrocytes and neurons. We now show that truncated species, lacking the LIM-type domain, retains the dimeric structure of the wild-type protein but exhibits a 10-fold increased kcat, a 3-fold decreased Km value for agmatine and altered intrinsic tryptophan fluorescent properties. As expected for a LIM protein, zinc was detected only in the wild-type ALP (∼2 Zn2+/monomer). Our proposal is that the LIM domain functions as an autoinhibitory entity and that inhibition is reversed by interaction of the domain with some yet undefined brain protein. |
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Keywords: | Agmatinase Polyamines LIM domain |
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