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

Tonoplast membrane of etiolated mung bean (Vinga radiata. L.) seedlings contained H+-translocating pyrophosphatase (PPase). Modification of tonoplast vesicles and partially purified PPase from etiolated mung bean seedlings with arginine-specific reagents, phenylglyoxal (PGO) and 2,3-butanedione (BD)...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1990-07, Vol.93 (3), p.1128-1133
Main Authors: Kuo, S.Y. (National Tsing Hua University, Taiwan, Repbulic of China), Pan, R.L
Format: Article
Language:English
Subjects:
Active sites
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Adenosine triphosphatases
AHILAMIENTO
ARGININA
ARGININE
Biological and medical sciences
CATION
CATIONES
Cell membranes
Cell physiology
Diphosphates
Enzymes
ETIOLEMENT
FOSFATOS
Fundamental and applied biological sciences. Psychology
HIDROGENO
HIDROLASAS
HIDROLISIS
HYDROGENE
HYDROLASE
HYDROLYSE
INHIBIDORES DE ENZIMAS
INHIBITEUR D'ENZYME
Kinetics
MEMBRANAS CELULARES
MEMBRANE CELLULAIRE
Membranes and Bioenergetics
PHOSPHATE
Phosphates
Plant physiology and development
PLANTULAS
PLANTULE
Plasma membrane and permeation
pyrophosphatase
Seedlings
Tonoplast
TRANSLOCACION
TRANSLOCATION
VACUOLA
VACUOLE
VIGNA RADIATA
Yeasts
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Description
Summary:Tonoplast membrane of etiolated mung bean (Vinga radiata. L.) seedlings contained H+-translocating pyrophosphatase (PPase). Modification of tonoplast vesicles and partially purified PPase from etiolated mung bean seedlings with arginine-specific reagents, phenylglyoxal (PGO) and 2,3-butanedione (BD), resultued in a marked decline in H+-translocating PPase activity. 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. The substrate, Mg2+-pryophosphate, provided partial protection against inactivation by these reagents. Loss of activity of partially purified PPase followed pseudo-first order kinetics. The double logarithm plots of pseudo-first order rate constant versus reagent concentrations gave slopes of 0.88 (PG0) and 0.90 (BD), rspectively, suggesting that the inactivation may possibly result from reaction of at least one arginyl residue at the active site of H+-translocating PPase
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.93.3.1128