Literature DB >> 7055584

Evidence for cooperative effects in human liver arginase.

N Carvajal, M Acoria, J P Rodríguez, M Fernández, J Martínez.   

Abstract

The reaction kinetics of human liver arginase (L-arginine amidinohydrolase, EC 3.5.3.1) in terms of arginine concentration is strikingly altered by varying the pH. Lowering the pH from the optimum (9.5) toward a more physiological value (7.5) there is a transition from hyperbolic to sigmoidal kinetics. The cooperative effects are observed in the presence and absence of the product ornithine. Dimers of arginase exhibit typical Michaelis-Menten kinetics even in the presence of ornithine. Dimer-dimer interactions are suggested to explain the kinetic properties of arginase at pH 7.5.

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Year:  1982        PMID: 7055584     DOI: 10.1016/0167-4838(82)90324-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

1.  Purification and Properties of the Constitutive Arginase of Evernia prunastri.

Authors:  A Martín-Falquina; M E Legaz
Journal:  Plant Physiol       Date:  1984-12       Impact factor: 8.340

2.  Purification and Properties of Arginase from Soybean, Glycine max, Axes.

Authors:  J H Kang; Y D Cho
Journal:  Plant Physiol       Date:  1990-07       Impact factor: 8.340

3.  Assaying ornithine and arginine decarboxylases in some plant species.

Authors:  H Birecka; A J Bitonti; P P McCann
Journal:  Plant Physiol       Date:  1985-10       Impact factor: 8.340

4.  Arginase of Helicobacter Gastric Pathogens Uses a Unique Set of Non-catalytic Residues for Catalysis.

Authors:  Ginto George; Mamata Kombrabail; Nikunj Raninga; Apurba Kumar Sau
Journal:  Biophys J       Date:  2017-03-28       Impact factor: 4.033

5.  Purification, properties and alternate substrate specificities of arginase from two different sources: Vigna catjang cotyledon and buffalo liver.

Authors:  Snehal Dabir; Pankaj Dabir; Baburao Somvanshi
Journal:  Int J Biol Sci       Date:  2005-08-01       Impact factor: 6.580

  5 in total

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