A novel protein from mung bean hypocotyl cell walls with acetyl esterase activity.
An acetyl esterase was purified from cell walls isolated from mung bean hypocotyls. The purified enzyme had an apparent Mr of 43,300 and an apparent pI > 9. It rapidly deesterified triacetin and p-nitrophenylacetate and slowly released acetate from beet and flax pectins, the deesterification rate being increased by previous demethylation of the pectins. No significant peptide sequence identity between the acetyl esterase and any known protein could be found in protein data bases.
Bordenave
M
M
Laboratoire d'Enzymologie en Milieu Structuré, Institut Jacques Monod, Paris, France.
Goldberg
R
R
Huet
J C
JC
Pernollet
J C
JC
D000115:Acetylesterase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D002473:Cell Wall / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D007887:Fabaceae / Q000201:enzymology*; D018546:Hypocotyl / Q000201:enzymology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010449:Peptide Mapping; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010946:Plants, Medicinal
D010446:Peptide Fragments; D010940:Plant Proteins; D000115:Acetylesterase