A Novel Sialidase Capable of Cleaving 3-Deoxy-D-glycero-D-galacto-2-nonulosonic Acid (KDN)

Li, Yu-Teh; Yuziuk, Jeffrey A.; Li, Su-Chen; Nematalla, Asaad; Hasegawa, Atsushi; Kimura, M.; Nakagawa, Hiroki

doi:10.1006/abbi.1994.1163

Cited by 26 publications

(22 citation statements)

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“…To validate the kinetics assay, we have used C. perfringens neuraminidase as standard for kinetic parameters measurement. According to the obtained results, C. perfringens Km equals to 89.2 µM for 4-MUNA, which is in a good accordance with the literature data of 120 µM (Li et al, 1994) (Inoue & Kitajima, 2006), while V max was detected to be 2856 µmol/min/mg. The obtained Km value of IgG were of similar range, while V max of IgG was significantly lower (k cat significantly higher) than that of C. perfringens neuraminidase.…”

Section: Wwwintechopencomsupporting

confidence: 89%

Cell Surface Glycans at SLE – Changes During Cells Death, Utilization for Disease Detection and Molecular Mechanism Underlying Their Modification

Rostyslav¹,

Tomin²,

Tolstyak³

et al. 2011

Autoimmune Disorders - Pathogenetic Aspects

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Section: Wwwintechopencomsupporting

confidence: 89%

Cell Surface Glycans at SLE – Changes During Cells Death, Utilization for Disease Detection and Molecular Mechanism Underlying Their Modification

Rostyslav¹,

Tomin²,

Tolstyak³

et al. 2011

Autoimmune Disorders - Pathogenetic Aspects

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“…Both enzymes were found to be stable between pH 3.5 and 7.2. The optimal pH for oyster KDN-sialidase is similar to that reported for KDN-sialidase from starfish, pH 4.0 (14), loach liver, pH 4.5 (13), and rainbow trout, pH 4.4 (32). The optimal pH for oyster KDNase is lower than that for S. multivorum KDNase, pH 5.7-6.0 (15).…”

Section: Purification Of Kdn-sialidase-supporting

confidence: 77%

“…The optimal pH for oyster KDNase is lower than that for S. multivorum KDNase, pH 5.7-6.0 (15). As shown in Table II, the K m (15.6 M) for the hydrolysis of MU-KDN by oyster KDN-sialidase is slightly smaller than those reported for other KDN-cleaving enzymes: 50 M for KDN-sialidase from starfish (14) and 70 M for loach KDN-sialidase (13).…”

Section: Purification Of Kdn-sialidase-mentioning

confidence: 66%

2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid (KDN)- and N-Acetylneuraminic Acid-cleaving Sialidase (KDN-sialidase) and KDN-cleaving Hydrolase (KDNase) from the Hepatopancreas of Oyster, Crassostrea virginica

Pavlova¹,

Yuziuk²,

Nakagawa³

et al. 1999

Journal of Biological Chemistry

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KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid), a sialic acid analog, has been found to be widely distributed in nature. Despite the structural similarity between KDN and Neu5Ac, ␣-ketosides of KDN are refractory to conventional sialidases. We found that the hepatopancreas of the oyster, Crassostrea virginica, contains two KDN-cleaving sialidases but is devoid of conventional sialidase. The major sialidase, KDN-sialidase, effectively cleaves ␣-ketosidically linked KDN and also slowly cleaves the ␣-ketosides of Neu5Ac. The minor sialidase, KDNase, is specific for ␣-ketosides of KDN. We were able to separate these two KDN-cleaving enzymes using hydrophobic interaction and cation-exchange chromatographies. The rate of hydrolysis of 4-methylumbelliferyl-␣-KDN (MU-KDN) by KDN-sialidase is 30 times faster than that of MU-Neu5Ac in the presence of 0.2 M NaCl, whereas in the absence of NaCl this ratio is only 8. KDNase hydrolyzes MU-KDN over 500 times faster than MU-Neu5Ac and is not affected by NaCl. KDN-sialidase purified to electrophoretically homogeneous form was found to have a molecular mass of 25 kDa and an isoelectric point of 8.4. One of the three tryptic peptides derived from KDN-sialidase contains the consensus motif, SXDXGXTW, that has been found in all conventional sialidases. Kinetic analysis of the inhibition of the hydrolysis of MU-KDN and MUNeu5Ac by 2,3-dehydro-2-deoxy-KDN (KDN2-en) and 2,3-dehydro-2-deoxy-(Neu5Ac2-en) suggests that KDN-sialidase contains two separate active sites for the hydrolysis of KDN and Neu5Ac. Both KDN-sialidase and KDNase effectively hydrolyze KDN-G M3 , KDN␣233Gal ␤134Glc, KDN␣236Gal␤134Glc, KDN␣236-N-acetylgalactosaminitol, KDN␣236(KDN␣233)N-acetylgalactosaminitol, and KDN␣236(GlcNAc␤133)N-acetylgalactosaminitol. However, only KDN-sialidase also slowly hydrolyzes G M3 , Neu5Ac␣233Gal␤134Glc, and Neu5Ac␣236Gal␤134Glc. These two KDN-cleaving sialidases should be useful for studying the structure and function of KDN-containing glycoconjugates.

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“…Significantly, KDNase Sm completely lacks any N-acylneuraminidase activity that releases Neu5Ac and Neu5Gc from a variety of Neu5Ac-and Neu5Gc-containing glycoconjugates (14). Studies from our group and from Li et al (13) describe the occurrence of "KDN sialidases" that cleave both KDN and N-acylneuraminyl ketosides in fish ovary (16) and liver (13).…”

Section: -Deoxy-d-galacto-d-glycero-nonulosonic Acid (Kdn)mentioning

confidence: 89%

“…Interestingly, immunochemical techniques suggested the presence of an oligomeric form of ␣238-linked KDN in mammalian tissues (10,11), and the occurrence of KDN residues was confirmed by biochemical and chemical methods (12). A unique feature of KDN-containing glycoconjugates is their complete resistance to the action of the known bacterial and viral exosialidases (1,5,9,13).…”

mentioning

confidence: 99%

Catalysis by a New Sialidase, Deaminoneuraminic Acid Residue-cleaving Enzyme (KDNase Sm), Initially Forms a Less Stable α-Anomer of 3-Deoxy-D-glycero-D-galacto-nonulosonic Acid and Is Strongly Inhibited by the Transition State Analogue, 2-Deoxy-2,3-didehydro-D-glycero-D-galacto-2-nonulopyranosonic Acid, but Not by 2-Deoxy-2,3-didehydro-N-acetylneuraminic Acid

Terada

Kitajima

Inoue

et al. 1997

Journal of Biological Chemistry

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Deaminoneuraminic acid residue-cleaving enzyme (KDNase Sm) is a new sialidase that has been induced and purified from Sphingobacterium multivorum. Catalysis by this new sialidase has been studied by enzyme kinetics and 1 H NMR spectroscopy. V max /K m values determined for synthetic and natural substrates of KDNase Sm reveal that 4-methylumbelliferyl-KDN (KDN␣2MeUmb, V max /K m ‫؍‬ 0.033 min ؊1 ) is the best substrate for this sialidase, presumably because of its good leaving group properties. The transition state analogue, 2,3-didehydro-2,3-dideoxy-D-galacto-D-glycero-nonulosonic acid, is a strong competitive inhibitor of KDNase Sm (K i ‫؍‬ 7.7 M versus K m ‫؍‬ 42 M for KDN␣2MeUmb). 2-Deoxy-2,3-didehydro-N-acetylneuraminic acid and 2-deoxy-2,3-didehydro-N-glycolylneuraminic acid are known to be strong competitive inhibitors for bacterial sialidases such as Arthrobacter ureafaciens sialidase; however, KDNase Sm activity is not significantly inhibited by these compounds. This observation suggests that the hydroxyl group at C-5 is important for recognition of the inhibitor by the enzyme.Reversible addition of water molecule (or hydroxide ion) to the reactive sialosyl cation, presumably formed at the catalytic site of KDNase Sm, eventually gives rise to two different adducts, the ␣-and ␤-anomers of free 3-deoxy-D-glycero-D-galacto-nonulosonic acid. 1 H NMR spectroscopic studies clearly demonstrate that the thermodynamically less stable ␣-form is preferentially formed as the first product of the cleavage reaction and that isomerization rapidly follows, leading to an equilibrium mixture of the two isomers, the ␤-isomer being the major species at equilibrium. Therefore, we propose that KDNase Sm catalysis proceeds via a mechanism common to the known exosialidases, but the recognition of the substituent at C-5 by the enzyme differs.

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A Novel Sialidase Capable of Cleaving 3-Deoxy-D-glycero-D-galacto-2-nonulosonic Acid (KDN)

Cited by 26 publications

References 0 publications

Cell Surface Glycans at SLE – Changes During Cells Death, Utilization for Disease Detection and Molecular Mechanism Underlying Their Modification

Cell Surface Glycans at SLE – Changes During Cells Death, Utilization for Disease Detection and Molecular Mechanism Underlying Their Modification

2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid (KDN)- and N-Acetylneuraminic Acid-cleaving Sialidase (KDN-sialidase) and KDN-cleaving Hydrolase (KDNase) from the Hepatopancreas of Oyster, Crassostrea virginica

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