In the course of solubilization and purification of fusicoccin binding sites present in microsomal fractions of spinach (Spinaciaoleracea L.)leaves,some endogenous hydrolases responsible for the poor stability of the receptors were identified [1]. Among them there was a serine proteinase displaying leucine-specific proteolytic activity.To reflect its primary specificity,the enzyme has been termed leucyl endopeptidase; other names are plantLeu-proteinase and leucine-specificserineproteinase [2,3]. In the absence of sequence and structural data,the enzyme cannot be assigned to a family,but it is likely to be in family S8. Leucyl endopeptidase activity has been detected in leaves, roots and seeds of Spinaciaoleracea L.
Aducci, P., Ascenzi, P. (2013). Leucyl endopeptidase. In N.D. Rawlings, G.S. Salvesen (a cura di), Handbook of proteolytic enzymes. 3rd ed. (pp. 3258-3260). Elsevier [10.1016/B978-0-12-382219-2.00719-5].
Leucyl endopeptidase
ADUCCI, PATRIZIA;
2013-01-01
Abstract
In the course of solubilization and purification of fusicoccin binding sites present in microsomal fractions of spinach (Spinaciaoleracea L.)leaves,some endogenous hydrolases responsible for the poor stability of the receptors were identified [1]. Among them there was a serine proteinase displaying leucine-specific proteolytic activity.To reflect its primary specificity,the enzyme has been termed leucyl endopeptidase; other names are plantLeu-proteinase and leucine-specificserineproteinase [2,3]. In the absence of sequence and structural data,the enzyme cannot be assigned to a family,but it is likely to be in family S8. Leucyl endopeptidase activity has been detected in leaves, roots and seeds of Spinaciaoleracea L.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
