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 k(cat), a 3-fold decreased K(m) 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 Zn(2+)/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.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Castro V,Fuentealba P,Henríquez A,Vallejos A,Benítez J,Lobos M,Díaz B,Carvajal N,Uribe Edoi
10.1016/j.abb.2011.05.003subject
Has Abstractpub_date
2011-08-01 00:00:00pages
107-10issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(11)00175-5journal_volume
512pub_type
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