Title : An essential arginyl residue in the tonoplast pyrophosphatase from etiolated mung bean seedlings.

Pub. Date : 1990 Jul

PMID : 16667568






3 Functional Relationships(s)
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1 The half-maximal inhibition was brought about by 20 millimolar PGO and 50 millimolar BD for membrane bound and 1.5 millimolar PGO and 5.0 millimolar BD for soluble PPase, respectively. Phenylglyoxal pyrophosphate-energized vacuolar membrane proton pump Vigna radiata
2 The half-maximal inhibition was brought about by 20 millimolar PGO and 50 millimolar BD for membrane bound and 1.5 millimolar PGO and 5.0 millimolar BD for soluble PPase, respectively. Phenylglyoxal pyrophosphate-energized vacuolar membrane proton pump Vigna radiata
3 The double logarithm plots of pseudo-first order rate constant versus reagent concentrations gave slopes of 0.88 (PGO) and 0.90 (BD), respectively, suggesting that the inactivation may possibly result from reaction of at least one arginyl residue at the active site of H(+)-translocating PPase. Phenylglyoxal pyrophosphate-energized vacuolar membrane proton pump Vigna radiata