Disease relevance of aspQ

• Amino acid utilization and urine protein excretion in children treated with succinylated Acinetobacter glutaminase-asparaginase [1].
• Two other enzymes, Erwinia L-asparaginase and succinylated Acinetobacter glutaminase-asparaginase, were cleared from the CSF at the same rate as bulk flow [2].
• Nitrogen utilization in mice bearing Ehrlich ascites tumor treated with Acinetobacter glutaminase-asparaginase [3].
• Tissue nitrogen-sparing effect of high protein diet in mice with or without ascites tumor treated with Acinetobacter glutaminase-asparaginase [4].
• Amino acid utilization was evaluated in seven children with acute lymphocytic leukemia treated with succinylated Acinetobacter glutaminase-asparaginase [1].

High impact information on aspQ

• Enhancement of antitumor activity of glutamine antagonists 6-diazo-5-oxo-L-norleucine and acivicin in cell culture by glutaminase-asparaginase [5].
• The combined actions of succinylated Acinetobacter glutaminase-asparaginase and 6-diazo-5-oxo-L-norleucine or Acivicin produced synergistic inhibition of nucleic acid synthesis in P388 tumor cells [5].
• Human pharmacology and toxicology of succinylated Acinetobacter glutaminase-asparaginase [6].
• The complete amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans, for which a preliminary tertiary structure is available from crystallographic analysis, has been determined by automated Edman degradation of fragments produced by chemical and proteolytic cleavages [7].
• Acinetobacter glutaminase-asparaginase was chemically modified by succinylation and glycosylation with glycopeptides from human fibrin and gamma-globulin [8].

Chemical compound and disease context of aspQ

• Pseudomonas 7 A glutaminase-asparaginase was treated with [6-14C]diazo-5-oxonorleucine and reduced with sodium borohydride [9].

Biological context of aspQ

• The present studies have demonstrated that another enzyme, Acinetobacter glutaminase-asparaginase (AGA) is much more effective in inhibiting cell growth [10].

Anatomical context of aspQ

• Our results demonstrate excessive central nervous system toxicity when glutaminase-asparaginase is administered on a daily schedule [11].

Associations of aspQ with chemical compounds

• Acinetobactor glutaminase-asparaginase was treated with [6-14C]diazo-5-oxonorleucine, reduced with sodium borohydride, and cleaved with cyanogen bromide [9].

References