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l-Rhamnulose 1-phosphate aldolase from Escherichia Coli. II. Characterization as a zinc metalloenzyme

✍ Scribed by Nancy B. Schwartz; David Sidney Feingold

Book ID: 104106038
Publisher: Elsevier Science
Year: 1972
Weight: 698 KB
Volume: 1
Category: Article
ISSN: 0006-3061
DOI: 10.1016/s0006-3061(00)80302-6

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✦ Synopsis

ARSTRACT ~Rhamnulose l-phosphate aldolase (n-rhamnulose l-phosphate ~-la&.aldehyde lyase, EC 4.1.2.b) was sensitive to inhibition by the metal chelators, S-hydroxyquinoliue, S-hydroxyquinoline-5-sulfonic acid, 1 , 10phenanthroline, and 2,2-bipyridine. The relative effectiveness of the inhibition paralleled the ability of the chelators to bid zinc. The activity of inhibited enzyme was restored by Z&II), Co(D), Ni(II), and Mn(II). Fe(D), hg(II), Cs(II), and Cu(II) did not restore activity. Atomic

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