N-acetylphenylalanyl-tRNA specific hydrolase in yeast

Bajo, M.; Moratilla, M.C.; Heredia, Claudio F.

doi:10.1016/s0006-291x(75)80037-4

Cited by 5 publications

(3 citation statements)

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“…The results in this paper describe the purification and properties of a yeast hydrolase previously found in this laboratory [7] that splits N-acetylphenylalanyltRNA to N-acetylphenylalanine plus tRNA. The enzyme has been extensively purified from the cytosol of yeast cells (Table 2 and Fig.…”

Section: Discussionmentioning

confidence: 87%

“…The N-acetylphenylalanyl-t RNA hydrolase activity was measured, unless otherwise stated, as described previously [7]. The assay for the peptidyl-tRNA hydrolase was basically the same except that N-acetyl-['"Clvalyl-tRNA was used as substrate.…”

Section: Assay For Enzymatic Activitiesmentioning

confidence: 99%

“…Enzymes of the first class are referred to as peptidyl-tRNA hydrolases because they also act on peptidyl-tRNAs. Among the enzymes of the second group, we previously reported the existence in yeast of a hydrolase which cleaves N-acetylphenylalanyl-tRNA to N-acetylphenylalanine plus tRNA [7]. An enzyme with these same characteristics was also found in encysted gastrulae and developing larvae of the crustacean Artemia salina [S].…”

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confidence: 99%

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N‐Acetylphenylalanyl‐tRNA Hydrolase from Yeast

Coloma

Heredia

1978

European Journal of Biochemistry

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This paper describes the purification and properties of an enzyme present in yeast which splits N‐acetylphenylalanyl‐tRNA to N‐acetylphenylalanine and tRNA. The enzyme has been extensively purified, as shown by gel electrophoresis. The hydrolase has a molecular weight of 35000 as estimated by filtration on Sephadex G‐150, is maximally active in the presence of a divalent cation (Mg2+, Mn2+ or Ca2+) and has a pH optimum at around neutrality. The enzyme is highly specific in hydrolyzing N‐acetylphenylalanyl‐tRNA (Km=0.4 μM). Phenylalanyl‐tRNA is hydrolyzed with a similar apparent affinity but with an efficiency of 40% of that found for N‐acetylphenylalanyl‐tRNA. Other free or N‐substituted aminoacyl‐tRNAs are not substrates of this hydrolase. Neither of the two reaction products are effective inhibitors of this enzyme. Based on its substrate specificity, the trivial name of N‐acetylphenylalanyl‐tRNA hydrolase is proposed for this enzyme.

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Section: Discussionmentioning

confidence: 87%

Section: Assay For Enzymatic Activitiesmentioning

confidence: 99%

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