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Biochem J
1996 May 01;315 ( Pt 3):1041-8. doi: 10.1042/bj3151041.
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Two different sialidases, KDN-sialidase and regular sialidase in the starfish Asterina pectinifera.
Yuziuk JA
,
Nakagawa H
,
Hasegawa A
,
Kiso M
,
Li SC
,
Li YT
.
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We have found the coexistence of two different sialidases in the entrails of the starfish Asterina pectinifera: a regular sialidase (RS), which cleaves sialic acid from sialoglycoconjugates, and a KDN-sialidase (KS) which releases the sialic acid analogue KDN (2-keto-3-deoxy-D-glycero-d-galacto-nononic acid) from KDN-containing glycoconjugates that are resistant to RS. The 6700-fold purified KS and 1300-fold purified RS were prepared to study the properties of these two sialidases. KS and RS from Asterina starfish differ in several properties other than glycon specificity, including molecular mass, isoelectric point (pI) and susceptibility to competitive and non-competitive inhibitors. KS has a molecular mass of 31 kDa and a pI of 8.3 while RS has a molecular mass of 128 kDa and a pI of about 4.8. 2,3-dehydro-2-deoxy-N-acetylneuraminic acid (NeuAc2en), but not 2,3-dehydro-2-deoxy-KDN (KDN2en), is a potent competitive inhibitor of RS (Ki approximately 0.007 mM); however, both NeuAc2en and KDN2en are moderate inhibitors of KS (K1 approximately 0.04 mM). Hg2+ is a potent non-competitive inhibitor of RS but not of KS. KS and RS were examined for their ability to hydrolyse KDN- and NeuAc-containing glycoconjugates. KS hydrolyses 4-methyl-umbelliferyl-alpha-KDN (MU-KDN) 20 times faster than 4-methylumbelliferyl-alpha-NeuAc (MU-NeuAc), while RS hydrolyses MU-NeuAc 88 times faster than MU-KDN at the pH optimum of 4.0 KS effectively hydrolyses KDN-GM3 (where GM3 is NeuAc alpha 2 --> 3Gal beta 1 --> 4Glc beta 1-1'' Cer, and Cer is ceramide), KDN alpha 2 --> 3lactose, KDN alpha 2 --> 6lactose, KDN alpha 2 --> 6N-acetylgalactosaminitol, KDN alpha 2 --> 6 (KDN alpha 2 --> 3)N-acetylgalactosaminitol and KDN alpha 2 --> 6(GlcNAc beta 1 --> 3) N-acetylgalactosaminitol. However, under the same conditions, these KDN-containing glycoconjugates are refractory to RS. Conversely, GM3, NeuAc alpha 2 --> 3lactose and NeuAc alpha 2 --> 6lactose are effectively hydrolysed by RS but not by KS.
Angata,
Identification, developmental expression and tissue distribution of deaminoneuraminate hydrolase (KDNase) activity in rainbow trout.
1994, Pubmed
Angata,
Identification, developmental expression and tissue distribution of deaminoneuraminate hydrolase (KDNase) activity in rainbow trout.
1994,
Pubmed
Heuermann,
Purification and characterization of a sialidase from Clostridium chauvoei NC08596.
1991,
Pubmed
Inoue,
KDN-glycoprotein: a novel deaminated neuraminic acid-rich glycoprotein isolated from vitelline envelope of rainbow trout eggs.
1988,
Pubmed
Kimura,
Characterization of a deaminated neuraminic acid-containing glycoprotein from the skin mucus of the loach, Misgurnus anguillicaudatus.
1994,
Pubmed
Kitajima,
Discovery of a new type of sialidase, "KDNase," which specifically hydrolyzes deaminoneuraminyl (3-deoxy-D-glycero-D-galacto-2-nonulosonic acid) but not N-acylneuraminyl linkages.
1994,
Pubmed
Kitazume,
Detection, isolation, and characterization of oligo/poly(sialic acid) and oligo/poly(deaminoneuraminic acid) units in glycoconjugates.
1992,
Pubmed
Knirel,
Structure of the capsular polysaccharide of Klebsiella ozaenae serotype K4 containing 3-deoxy-D-glycero-D-galacto-nonulosonic acid.
1989,
Pubmed
Li,
A novel sialidase capable of cleaving 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid (KDN).
1994,
Pubmed
Moore,
Use of azo-dye-bound collagen to measure reaction velocities of proteolytic enzymes.
1969,
Pubmed
Murayama,
Fluorimetric assay of sialic acids.
1976,
Pubmed
Myers,
The synthesis of 4-methylumbelliferyl alpha-ketoside of N-acetylneuraminic acid and its use in a fluorometric assay for neuraminidase.
1980,
Pubmed
Nadano,
A naturally occurring deaminated neuraminic acid, 3-deoxy-D-glycero-D-galacto-nonulosonic acid (KDN). Its unique occurrence at the nonreducing ends of oligosialyl chains in polysialoglycoprotein of rainbow trout eggs.
1986,
Pubmed
Nakagawa,
Purification and characterization of alpha-N-acetylgalactosaminidase from skipjack liver.
1987,
Pubmed
Potier,
Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate.
1979,
Pubmed
Schauer,
Isolation and characterization of a sialidase from the starfish Asterias rubens.
1989,
Pubmed
,
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Smith,
Measurement of protein using bicinchoninic acid.
1985,
Pubmed
Song,
Isolation and structural elucidation of a novel type of ganglioside, deaminated neuraminic acid (KDN)-containing glycosphingolipid, from rainbow trout sperm. The first example of the natural occurrence of KDN-ganglioside, (KDN)GM3.
1991,
Pubmed
Strecker,
Characterization of Le(x), Le(y) and A Le(y) antigen determinants in KDN-containing O-linked glycan chains from Pleurodeles waltlii jelly coat eggs.
1992,
Pubmed
Tronsmo,
Detection and quantification of N-acetyl-beta-D-glucosaminidase, chitobiosidase, and endochitinase in solutions and on gels.
1993,
Pubmed
