Insight on the interaction of an agmatinase-like protein with Mn(2 +) activator ions

Quiñones, Matías, Cofre, Jaime, Benítez, José, García, David, Romero, Nicol, González, Arlette, Carvajal, Nelson, García, María, López, Vasthi, Schenk, Gerhard and Uribe, Elena (2015) Insight on the interaction of an agmatinase-like protein with Mn(2 +) activator ions. Journal of Inorganic Biochemistry, 145 65-69. doi:10.1016/j.jinorgbio.2015.01.008

Author Quiñones, Matías
Cofre, Jaime
Benítez, José
García, David
Romero, Nicol
González, Arlette
Carvajal, Nelson
García, María
López, Vasthi
Schenk, Gerhard
Uribe, Elena
Title Insight on the interaction of an agmatinase-like protein with Mn(2 +) activator ions
Formatted title
Insight on the interaction of an agmatinase-like protein with Mn2 + activator ions
Journal name Journal of Inorganic Biochemistry   Check publisher's open access policy
ISSN 0162-0134
Publication date 2015-04
Sub-type Article (original research)
DOI 10.1016/j.jinorgbio.2015.01.008
Open Access Status
Volume 145
Start page 65
End page 69
Total pages 5
Place of publication Philadelphia, PA, United States
Publisher Elsevier
Collection year 2016
Language eng
Formatted abstract
• Interactions of an agmatinase-like protein (ALP) with Mn2 + were analyzed.
• Histidine residues were replaced to identify the Mn2 + binding site.
• ALP has one tightly bound Mn2 + and is active in mononuclear form.
• Formation of a binuclear Mn2 + center is promoted at high temperatures.
• Formation of a binuclear Mn2 + center increases both activity and enzyme stability.

Agmatinase is an enzyme that catalyzes the hydrolysis of agmatine, a compound that is associated with numerous functions in the brain of mammalian organisms such as neurotransmitter, anticonvulsant, antinociceptive, anxiolytic and antidepressant-like actions. To date the only characterized agmatinases with significant enzymatic activity were extracted from bacterial organisms. These agmatinases are closely related to another ureahydrolase, arginase; both have binuclear Mn2 + centers in their active sites. An agmatinase-like protein (ALP) from rat brain was identified that bears no sequence homology to known agmatinases (E. Uribe, M. Salas, S. Enriquez, M.S. Orellana, N. Carvajal, Arch. Biochem. Biophys. 461(2007) 146–150). Since all known ureahydrolases contain histidines in their binuclear Mn2 + site each of the five histidine residues in ALP was individually replaced by alanines to identify those that may be involved in metal ion binding. Reactivation assays and thermal stability measurements indicated that His206 is likely to interact with a Mn2 + bound to a high affinity site. In contrast, His65 and possibly His435 are important for binding of a second Mn2 + to a lower affinity site. Metal ion binding to that site is not only leading to an increase in reactivity but also enzyme stability. Thus, similar to bacterial agmatinases and some of the antibiotic-degrading, Zn2 +-dependent metallo-β-lactamases ALP appears to be active in the mono and binuclear form, with binding of the second metal ion increasing both reactivity and stability.
Keyword Agmatine
Agmatinase like protein
Mn 2+ ions
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Chemistry and Molecular Biosciences
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Created: Fri, 06 Feb 2015, 09:39:19 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences