Neuraminidase and N-Acetylneuraminate Pyruvate-Lyase of Pasteurella multocida

Drzeniek, R.; Scharmann, W.; Balke, Erika

doi:10.1099/00221287-72-2-357

Cited by 34 publications

(31 citation statements)

References 12 publications

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“…Scharmann et al (1970) reported that most strains of/ 3 , haemolytica and P. multocida produce the enzyme. These results were later verified by other investigators (Drzeniek et al, 1972;Frank & Tabatabai, 1981;Straus et al, 1996). These studies were primarily designed to determine which Pasteurella species produced the enzyme and if any differences in production existed between the serotypes (Frank & Tabatabai, 1981;Straus et al, 1993Straus et al, , 1996.…”

Section: Neuraminidasesupporting

confidence: 78%

“…These studies were primarily designed to determine which Pasteurella species produced the enzyme and if any differences in production existed between the serotypes (Frank & Tabatabai, 1981;Straus et al, 1993Straus et al, , 1996. Characterization of the neuraminidase produced by P. haemolytica and P. multocida has also received some attention (Drzeniek et al, 1972;Straus et al, 1996;White et al, 1995). On the basis of these investigations, it appears that neuraminidase production is common to all somatic and capsule serovars (except F) of P. multocida and that the enzyme of P. multocida differs from that of other organisms by having a higher molecular weight.…”

Section: Neuraminidasementioning

confidence: 99%

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Avian pasteurellosis: Taxonomy of the organisms involved and aspects of pathogenesis

Christensen

Bisgaard

1997

Avian Pathology

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Section: Neuraminidasesupporting

confidence: 78%

Section: Neuraminidasementioning

confidence: 99%

Avian pasteurellosis: Taxonomy of the organisms involved and aspects of pathogenesis

Christensen

Bisgaard

1997

Avian Pathology

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“…The X-ray structures of NanA from E. coli and Haemophilus influenzae have been solved (Barbosa et al 2000;Izard et al 1994;Lawrence et al 1997). NanA activity has been found in Pasteurella multocida (Drzeniek et al 1972) and a hypothetic gene sequence encoding NanA (Pm1715, GenBank accession no. Q9CKB0) has been identified (Steenbergen et al 2005).…”

Section: Reactionmentioning

confidence: 99%

Pasteurella multocida sialic acid aldolase: a promising biocatalyst

Cao

et al. 2008

Appl Microbiol Biotechnol

117

151

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Sialic acid aldolases or N-acetylneuraminate lyases (NanAs) catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) to form pyruvate and N-acetyl-D-mannosamine (ManNAc). A capillary electrophoresis (CE) assay was developed to directly characterize the activities of NanAs in both Neu5Ac cleavage and Neu5Ac synthesis directions. The assay was used to obtain the pH profile and the kinetic data of a NanA cloned from Pasteurella multocida P-1059 (PmNanA) and a previously reported recombinant Escherichia coli K12 NanA (EcNanA). Both enzymes are active in a broad pH range of 6.0-9.0 in both reaction directions and have similar kinetic parameters. Substrates specificity studies showed that 5-O-methyl-ManNAc, a ManNAc derivative, can be used efficiently as a substrate by PmNanA, but not efficiently by EcNanA, for the synthesis of 8-O-methyl Neu5Ac. In addition, PmNanA (250 mg per liter culture) has a higher expression level (2.5 fold) than EcNanA (94 mg per liter culture). The higher expression level and a broader substrate tolerance make PmNanA a better catalyst than EcNanA for the chemoenzymatic synthesis of sialic acids and their derivatives.

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“…G. FRASER AND J. K. SMITH Cassidy et al (1965) found that the NANA in al-acid glycoprotein could be completely released by C. weichii neuraminidase and that the initial rate of release was slightly faster than the initial rate of release from bovine NAN-lactose. About 80% of the NAN-lactose in bovine colostrum is N-acetyl neuramin-(2-+3)-lactose but the (2--+6) isomer is also present (Schneir and Rafelson, 1966;Drzeniek, 1973). Viral neuraminidases may show a marked difference in ability to hydrolyse (2+3) and ( 2 4 ) linkages; both linkages are completely hydrolysed by C. welchii or V. cholerae neuraminidase although the rate of the reaction is rather slower with the (2-4 isomer (Cassidy et al, 1965;Drzeniek, 1967).…”

Section: Discussionmentioning

confidence: 99%

“…Viral neuraminidases may show a marked difference in ability to hydrolyse (2+3) and ( 2 4 ) linkages; both linkages are completely hydrolysed by C. welchii or V. cholerae neuraminidase although the rate of the reaction is rather slower with the (2-4 isomer (Cassidy et al, 1965;Drzeniek, 1967). In al-acid glycoprotein, NANA is linked to the carbohydrate side chains by both (2-3) and (2-26) linkages (Drzeniek, 1973).…”

Section: Discussionmentioning

confidence: 99%