Taxonomic distribution of proteins containing Asparaginase domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Asparaginase domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB,and its regulation by cyclic AMP receptor and FNR proteins.

Jennings MP, Beacham IR
J Bacteriol. 1990; 172: 1491-8

Escherichia coli contains two L-asparaginase isozymes: L-asparaginase I, alow-affinity enzyme located in the cytoplasm, and L-asparaginase II, ahigh-affinity secreted enzyme. A molecular genetic analysis of the gene(ansA) encoding the former enzyme has previously been reported. We nowpresent a molecular study of the gene, ansB, encoding L-asparaginase II.This gene was isolated by using oligonucleotide probes, whose sequenceswere based on the previously determined amino acid sequence. Thenucleotide sequence of ansB, including 5'- and 3'-untranslated regions,was determined. The amino acid sequence of L-asparaginase II, deduced fromthis nucleotide sequence, contains differences at 11 positions whencompared with the previously determined amino acid sequence. The deducedamino acid sequence also reveals a typical secretory signal peptide of 22residues. A single region of sequence similarity is observed when ansA andansB are compared. The transcriptional start site in ansB was determined,allowing the identification of the promoter region. The regulation of ansBwas studied by using ansB'-'lacZ fusions, together with a deletionanalysis of the 5' region upstream of the promoter. Regulation by cyclicAMP receptor protein and anaerobiosis (FNR protein) was confirmed, and thepresence of nucleotide sequence motifs, with homology to cyclic AMPreceptor protein and FNR protein-binding sites, investigated.

Structures of amidohydrolases. Amino acid sequence of aglutaminase-asparaginase from Acinetobacter glutaminasificans andpreliminary crystallographic data for an asparaginase from Erwiniachrysanthemi.

Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A
J Biol Chem. 1988; 263: 8583-91

The complete amino acid sequence of a glutaminase-asparaginase fromAcinetobacter glutaminasificans, for which a preliminary tertiarystructure is available from crystallographic analysis, has been determinedby automated Edman degradation of fragments produced by chemical andproteolytic cleavages. The protein consists of 331 amino acid residues andhas a molecular weight of 35,500. The pattern of hydrophilic andhydrophobic regions is typical of a globular protein. A new crystal formof an Erwinia chrysanthemi 1125 asparaginase is reported. The space groupis monoclinic C2, with unit cell parameters of: a = 107.8, b = 91.7, c =129.2 A and beta = 91.7 degrees. A Vm of 2.25 A3/dalton was calculated forone tetramer of 35,100-dalton subunits per asymmetric unit. X-rayintensity data have been obtained to 2.2 A resolution. The point groupsymmetry of the Er. chrysanthemi tetramer is 222 from self-rotationfunction calculations. The relative orientations of an A.glutaminasificans glutaminase-asparaginase model and the Er. chrysanthemiasparaginase tetramer have been determined with the cross-rotationfunction, and translation function calculations have revealed a plausiblelocation for the asparaginase tetramer in the crystal.

Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 L-asparaginasegene.

Minton NP, Bullman HM, Scawen MD, Atkinson T, Gilbert HJ
Gene. 1986; 46: 25-35

The complete nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066gene coding for the chemotherapeutic enzyme L-asparaginase has beendetermined. The structural gene consists of an open reading framecommencing with an ATG start codon of 1044 bp followed by a TGA stopcodon. Confirmation of the nucleotide sequence was obtained by comparingthe predicted amino acid (aa) sequence with that derived by N-terminal aasequencing of the purified protein. The gene has been shown to code for a21-aa signal peptide at its N terminus which closely resembles the signalpeptides of other secreted proteins. In common with highly expressedEscherichia coli genes, little use is made of modulator codons. Thepredicted aa sequence of the enzyme exhibits 46% identity with thedetermined primary sequence of the E. coli L-asparaginase, although thepredicted secondary structure of both proteins indicates more extensivehomology. Downstream of the TGA stop codon is a G + C-rich region of dyadsymmetry (delta G = -25.4 kcal) characteristic of E. coli Rho-independenttranscription terminators. Upstream of the structural gene there are nosequences which bear a strong resemblance to the consensus -35 and -10regions of E. coli promoters. A sequence is present (CTGGCTCTCCTCTTGAT),however, which exhibits strong homology to the nif promoter consensussequence (CTGGCACN5TTGCA). Upstream of this region is a sequence whichstrongly resembles the consensus sequence for promoter regions which aresubject to catabolite repression.