Observations Upon the Enzyme Asparaginase

Geddes, W. F.; Hunter, Andrew

doi:10.1016/s0021-9258(18)84052-2

Cited by 24 publications

(4 citation statements)

References 10 publications

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“…This paper reports a parallel study in which we have examined the activity of various enzyme preparations, especially those from rabbit liver, in hydrolyzing the carbamyl group. Similar investigations are those of Gonnermann (1902,1903), in which the action of several enzyme preparations, including pepsin, trypsin and sheep's liver and kidney, on a number of amides and anilides was studied, of Geddes & Hunter (1928) and of Grassmann & Mayr (1933) who examined the action ofyeast asparaginase on several amides. The criterion used by Gonnermann as an indication of hydrolysis was the isolation of the unchanged amide or of products of its hydrolysis, whilst Geddes & Hunter estimated the ammonia liberated.…”

supporting

confidence: 64%

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The fate of certain organic acids and amides in the rabbit

Bray

James

Ryman

et al. 1948

Biochemical Journal

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supporting

confidence: 64%

“…Table 1. Summary of re8uWtt of some prev'ou8 inve8tigation8 of enzymic hydroly8i8 of amide8 (Results marked * due to Geddes & Hunter (1928). Results marked t due to Grassmann & Mayr (1933).…”

Section: Amide8mentioning

confidence: 99%

The fate of certain organic acids and amides in the rabbit

Bray

James

Ryman

et al. 1948

Biochemical Journal

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“…This humble chemical reaction contrasts with the picturesque history of discovery of this amazingly diverse group of enzymes, which starts at the beginning of the 20th century with the observation of the existence of amide-splitting enzymes in suspensions of animal and plant tissues (Gonnermann, 1902). However, these early observations did not refer directly to the hydrolysis of l-asparagine (Geddes & Hunter, 1928; Fig. 1).…”

Section: Asparaginases: Historical Facts and Structure-based Classificationmentioning

confidence: 97%

Structural and biophysical aspects of L-asparaginases: a growing family with amazing diversity

Loch

Jaskólski

2021

IUCrJ

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L-Asparaginases have remained an intriguing research topic since their discovery ∼120 years ago, especially after their introduction in the 1960s as very efficient antileukemic drugs. In addition to bacterial asparaginases, which are still used to treat childhood leukemia, enzymes of plant and mammalian origin are now also known. They have all been structurally characterized by crystallography, in some cases at outstanding resolution. The structural data have also shed light on the mechanistic details of these deceptively simple enzymes. Yet, despite all this progress, no better therapeutic agents have been found to beat bacterial asparaginases. However, a new option might arise with the discovery of yet another type of asparaginase, those from symbiotic nitrogen-fixing Rhizobia, and with progress in the protein engineering of enzymes with desired properties. This review surveys the field of structural biology of L-asparaginases, focusing on the mechanistic aspects of the well established types and speculating about the potential of the new members of this amazingly diversified family.

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“…Clementi (1922) was the first to observe the presence of L-asparaginase in several of the tissues of herbivorous animals. Geddes & Hunter (1928) later observed the presence of L-asparaginase in calf liver. Our studies show that ox liver contains low L-asparaginase activity compared with the liver of the other species studied (3.6,umol/h per g).…”

Section: Pancreas Livermentioning

confidence: 96%

The distribution of l-asparagine synthetase in the principal organs of several mammalian and avian species

Milman

Cooney

1974

Biochemical Journal

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A survey was conducted of the distribution of l-asparagine synthetase and of l-asparaginase in the principal organs of representative mammals and birds. Although a radiometric assay was used as a routine, several additional criteria, including enzymic and chromatographic ones, were used to verify that the product of the synthetase was l-asparagine. Recoveries of exogenous l-asparagine were assessed in the presence of a number of mouse organs and found to be about 85%. In addition, evidence is presented for the existence in mouse liver of a thermolabile activity capable of destroying l-asparagine and stimulated by high concentrations of NH(4) (+) ions. Of the organs surveyed, pancreas was generally found to synthesize l-asparagine at the most rapid rate, whereas extracts of liver catalysed the decomposition of this amide at the greatest velocity. Of the species studied, guinea pig had the highest activities of pancreatic l-asparagine synthetase and also of hepatic l-asparaginase. The pancreas of mouse and ox also were good sources of l-asparagine synthetase.

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Observations Upon the Enzyme Asparaginase

Cited by 24 publications

References 10 publications

The fate of certain organic acids and amides in the rabbit

The fate of certain organic acids and amides in the rabbit

Structural and biophysical aspects of L-asparaginases: a growing family with amazing diversity

The distribution of l-asparagine synthetase in the principal organs of several mammalian and avian species

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