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PLA2G1B — TYRP1

Text-mined interactions from Literome

Sumandea et al., Biochemistry 1999 : Binding affinities of the mutants for phospholipid coated beads and their monolayer penetration indicate that Trp-19 , Trp-61, and Phe-64 are critically involved in interfacial binding of N. n. atra PLA2 and penetrate into the membrane during the interfacial catalysis of N. n. atra PLA2
Chang et al., Biochim Biophys Acta 1993 : Modification of Trp-19 and Trp-61 resulted in a decrease in enzymatic activity of PLA2 by 45.5 % and 51 %, respectively ... These observations, together with the fact that Trp-18 is involved in the substrate binding of PLA2 , suggest that incorporation of a bulky NPS group on Trp-18 might give rise to a direct distortion of the interaction between substrate and the enzyme molecule ... Alternatively, modification of Trp-19 and Trp-61 might indirectly affect the interfacial binding of PLA2 with its substrate