Partial purification of bacterial aspartase by starch electrophoresis

Wilkinson, Jack S.; Williams, Virginia R.

doi:10.1016/0003-9861(61)90318-6

Cited by 22 publications

(11 citation statements)

References 6 publications

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“…74 Only in 1971 was the enzyme responsible for this activity (EcDAL, also known as AspA) isolated and purified from E. coli. 75 Even though AspA remains the most studied member of the aspartase family, several other DALs have been isolated from various sources, for instance Pseudomonas f luorescens, 76 Hafnia alveis (formerly known as Bacterium cadaveris), 77 Aeromonas media, 78 Bacillus subtilis, 79 and Bacillus sp. YM55-1 (also known as AspB).…”

Section: Structure and Mechanism Of Aspartatementioning

confidence: 99%

Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases

et al. 2017

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Ammonia-lyases and aminomutases are mechanistically and structurally diverse enzymes which catalyze the deamination and/or isomerization of amino acids in nature by cleaving or shifting a C-N bond. Of the many protein families in which these enzyme activities are found, only a subset have been employed in the synthesis of optically pure fine chemicals or in medical applications. This review covers the natural diversity of these enzymes, highlighting particular enzyme classes that are used within industrial and medical biotechnology. These highlights detail the discovery and mechanistic investigations of these commercially relevant enzymes, along with comparisons of their various applications as stand-alone catalysts, components of artificial biosynthetic pathways and biocatalytic or chemoenzymatic cascades, and therapeutic tools for the potential treatment of various pathologies.

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Section: Structure and Mechanism Of Aspartatementioning

confidence: 99%

Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases

et al. 2017

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“…For all three phage T4 introns, plots indicate competitive inhibition at both low salt concentrations and at the salt maxima (not shown). In the Hanes-Woolf plot, measurements at different [GTP] have similar statistical weights (similar errors) so that the best fitting lines are intuitively apparent (Wilkinson, 1961): amol, 10-18 moles; fmol, 10-15 moles.…”

Section: Amino Acid Surveysmentioning

confidence: 99%

Stereoselective arginine binding is a phylogenetically conserved property of group I self-splicing RNAs.

1989

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We have examined the reaction of GTP with RNA polymerase transcripts containing the self‐splicing RNA precursors from the Neurospora crassa Cob1 intron, and from introns in the sunY, nrdB and td genes of bacteriophage T4. In each case, we find a low Km for GTP (between 0.8 and 11 microM), accompanied by competitive inhibition of the GTP reaction by L‐arginine, as was found for the previously examined Tetrahymena nuclear pre‐rRNA intron. Trials with the 20 standard amino acids show that inhibition in all cases is specific to the arginine side‐chain. L‐arginine binds with similar affinity to all introns studied, the Ki's ranging from 4.3 to 21 mM. Strikingly, the relative binding preference of the RNAs for L‐ versus D‐arginine is highly conserved: the ratio of L‐arg Ki/D‐arg Ki, the stereoselectivity, is always close to 2. Because of the conservation of GTP and arginine binding constants and particularly because of the conserved stereoselectivity, we conclude that the evolution of an effective group I RNA transesterification catalyst necessarily produces a specific and stereoselective RNA binding site for a single amino acid. This suggests that selection for an ancient group I RNA could have fortuitously initiated the specific association of RNA sequences with amino acids, a first step toward the genetic code.

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“…The enzyme catalytic action depends upon free sulfhydryl groups located at the active sites, the oxidation of which inactivates the enzyme (Depue and Moat, 1961;Mizuta and Tokushige, 1975). There have been several reports on the divalent metal ion activation of aspartase (Ichihara et al, 1955;Wilkinson and Williams, 1961). Aspartase is reported to contain or require divalent metal ions possibly an alkaline earth metal (Mg), to be active above neutral pH (Rudolph and Fromm, 1971).…”

Section: Amidohydrolases In Soilsmentioning

confidence: 99%

Amino acid composition of soil organic matter and nitrogen transformations in soils under different management systems

Senwo

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Partial purification of bacterial aspartase by starch electrophoresis

Cited by 22 publications

References 6 publications

Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases

Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases

Stereoselective arginine binding is a phylogenetically conserved property of group I self-splicing RNAs.

Amino acid composition of soil organic matter and nitrogen transformations in soils under different management systems

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