Disease relevance of nanA

• Cloning, sequence, and transcriptional regulation of the operon encoding a putative N-acetylmannosamine-6-phosphate epimerase (nanE) and sialic acid lyase (nanA) in Clostridium perfringens [1].
• The regulation of the neuraminidase gene nanA was examined in Pseudomonas and as cloned and expressed in Escherichia coli [2].
• Under the hyperosmolar conditions postulated to exist in the CF lung, nanA is likely to be expressed to facilitate the initial adherence of Pseudomonas to the respiratory tract [2].

High impact information on nanA

• To identify proteins that might be involved in recognition of nuclear localization signals, we isolated conditional-lethal mutants (npl, for nuclear protein localization) that missorted NLS-cytochrome c1 to the mitochondria, allowing growth on glycerol [3].
• Complete nucleotide sequence of the E. coli N-acetylneuraminate lyase [4].
• Several signal sequences conserved in the promoter regions of E. coli were found in the npl gene [4].
• In order to understand the nature of this intermediate, we have determined the three-dimensional structure of N-acetylneuraminate lyase in complex with hydroxypyruvate (a product analogue) and in complex with one of its products (pyruvate) [5].
• Although these substituents are considered to protect the chains against degradation by bacterial glycosidases, sialate O-acetylesterase, N-acetylneuraminate lyase, and glycosulfatase activities have been found in fecal extracts [6].

Biological context of nanA

• An open reading frame beginning 135 bp from the nanA translational stop codon could code for a 53,547-Da hydrophobic polypeptide predicted to contain 14 transmembrane segments [7].
• By using Northern blot experiments, it was demonstrated that the nanE and nanA genes comprise an operon and that transcription of the operon in C. perfringens is inducible by the addition of sialic acid to the growth medium [1].
• A model gene, N-acetylneuraminate lyase gene (nanA), fused with the promoter region of Escherichia coli lac operon successfully overproduced the protein independently from the inducer [8].
• Two plasmids containing the N-acetylneuraminate lyase (NALase) gene (nanA) of Escherichia coli, pNL1 and pNL4, were constructed [9].
• Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: insights into the reaction mechanism [10].

Associations of nanA with chemical compounds

• The nanA gene product was also shown to restore growth to EV78 in minimal medium with sialic acid as the sole carbon source [1].
• The Northern blot experiments also showed that there is no catabolite repression of nanE-nanA transcription by glucose [1].
• The function of the sialate aldolase (encoded by nanA) in limiting intermediate flux through the synthetic pathway was determined by analyzing free sialate accumulation in neuA (CMP-sialic acid synthetase) nanA double mutants [11].
• BACKGROUND: N-acetylneuraminate lyase catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine [12].

Other interactions of nanA

• Among the sugars tested that were predicted to be products of the nan-encoded system, only the exogenous addition of sialic acid resulted in the dramatic induction of a chromosomal nanA-lacZ fusion or displaced NanR from its operator in vitro [13].

Analytical, diagnostic and therapeutic context of nanA

• Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli [14].

References