Disease relevance of NGO0949

• Hydrolases from Neisseria gonorrhoeae. The study of gonocosin, an aminopeptidase-P, a proline iminopeptidase, and an asparaginase [1].
• Escherichia coli clones expressing the gonococcal gene coding for Pip were identified in a genomic cosmid library using a synthetic colorimetric substrate [2].
• Proline iminopeptidase gene from Xanthomonas campestris pv. citri [3].

High impact information on NGO0949

• Complementation of an E. coli mutant deficient in both proline biosynthesis and dipeptide uptake confirmed that Pip is capable of releasing biologically active proline from peptides [2].
• Nucleotide sequence determination and analyses of polypeptides detected by coupled in vitro transcription/translation reactions revealed that Pip is a 311-amino-acid polypeptide with a M(r) of 35 kDa and a pI of 5 [2].
• The XAP gene product, Xap, expressed in Escherichia coli has proline iminopeptidase activity as well as ascamycin dealanylating activity in vitro [4].
• The deduced amino acid sequence showed 47% identity with the Pip from Neisseria gonorrhoeae [3].
• The pip gene coding for the proline iminopeptidase (Pip) of Xanthomonas campestris pv. citri was cloned in an Escherichia coli leuB strain using a selective medium containing the dipeptide D-Ala-L-Leu as the sole source of L-leucine [3].

Analytical, diagnostic and therapeutic context of NGO0949

• Molecular cloning and characterization of a proline iminopeptidase gene from Neisseria gonorrhoeae [2].
• Sequence analysis reveals that the gene encodes a 311 amino acid protein with a calculated molecular mass of 35134 Da and approx. 50% identity for amino acids to the proline iminopeptidase from Neisseria gonorrhoeae [4].
• The molecular mass of Pip was found to be 35 kDa by SDS-PAGE and 120 kDa by gel filtration, suggesting that the active enzyme is a multimer [3].

References