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CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
CMP-N-acetylneuraminate + 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + O2
CMP-N-glycoloylneuraminate + ?
-
less effectiove than NADH or NADPH
-
-
?
CMP-N-acetylneuraminate + ascorbic acid + O2
CMP-N-glycoloylneuraminate + dehydroascorbate + H2O
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
CMP-N-acetylneuraminate + NADPH + O2
CMP-N-glycoloylneuraminate + NADP+ + H2O
additional information
?
-
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
?
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + ascorbic acid + O2
CMP-N-glycoloylneuraminate + dehydroascorbate + H2O
-
ascorbate is ineffective
-
-
?
CMP-N-acetylneuraminate + ascorbic acid + O2
CMP-N-glycoloylneuraminate + dehydroascorbate + H2O
-
less effective than NADH or NADPH
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
evidence for the formation of a ternary complex of hydroxylase, CMP-Neu5Ac and cytochrome b5
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
pure hydrophilic cytochrome b5 interacts more effectively with the hydroxylase than isolated amphiphytic cytochrome b5
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
2 electrons are donated by either NADH or NADPH are transported via cytochrome b5 in the CMP-NeuAc hydroxylation system of mouse liver cytosol
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
the electron carrier cytochrome b5 is essential for activity
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2
CMP-N-glycoloylneuraminate + ferricytrochrome b5 + H2O
-
pure hydrophilic cytochrome b5 interacts more effectively with the hydroxylase than isolated amphiphytic cytochrome b5
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
-
the enzyme determines the sugar bound to the red cell by converting NeuAc to NeuGc. Thus, mutations in CMAH may cause the A and B blood types, two major serotypes. Blood type A is dominant to type B. A rare type AB may also be allelic and is suspected to be recessive to A and dominant to B. Cat blood type antigens are defined: N-glycolylneuraminic acid, NeuGc, is associated with type A and N-acetylneuraminic acid, NeuAc, with type B, overview
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
C1K3L2
-
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
-
-
-
-
ir
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
the enzyme is the key for regulation of the overall velocity of CMP-NeuAc hydroxylation and consequently for the expression of N-glycoloylneuraminic acid glycoconjugates
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
a regulation of CMP-N-acetylneuraminate hydroxylation and thus the ratio of glycoconjugate-bound N-acetylneuraminate and N-acetylglycoloylneuraminate might occur by varying the amount of hydroxylase protein within the cell, possibly by controlling the expression of the hydroxylase gene
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
the enzyme plays a decisive role in governing the relative amounts of N-acetylneuraminate and N-acetylglycolylneuraminate occuring in the glycoconjugates of a tissue
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
key enzyme for the expression of N-glycoloylneuraminic acid
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
NADPH and NADH are by far the most effective cofactors
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
the biosynthesis of the sialic acid N-glycolylneuraminic acid occurs by the action of cytidine monophosphate-N-acetylneuraminate hydroxylase. Incorporation of N-glycoloylneuraminic acid into glycoconjugates is generally controlled by the amount of hydroxylase protein expressed in a tissue
-
-
?
CMP-N-acetylneuraminate + NADPH + O2
CMP-N-glycoloylneuraminate + NADP+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADPH + O2
CMP-N-glycoloylneuraminate + NADP+ + H2O
-
binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid
-
-
?
CMP-N-acetylneuraminate + NADPH + O2
CMP-N-glycoloylneuraminate + NADP+ + H2O
-
NADPH and NADH are by far the most effective cofactors
-
-
?
additional information
?
-
-
no activity towards free or alpha-glycosidically bound N-acetylneuraminic acid
-
-
?
additional information
?
-
ectopic expression of pcmah in pig kidney PK15 cells and human vascular endothelial ECV304 cells leads to an elevated expression of N-glycolylneuraminic acid
-
-
?
additional information
?
-
-
ectopic expression of pcmah in pig kidney PK15 cells and human vascular endothelial ECV304 cells leads to an elevated expression of N-glycolylneuraminic acid
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
?
CMP-N-acetylneuraminate + 2 ferrocytochrome b5 + O2 + 2 H+
CMP-N-glycoloylneuraminate + 2 ferricytochrome b5 + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
-
the enzyme determines the sugar bound to the red cell by converting NeuAc to NeuGc. Thus, mutations in CMAH may cause the A and B blood types, two major serotypes. Blood type A is dominant to type B. A rare type AB may also be allelic and is suspected to be recessive to A and dominant to B. Cat blood type antigens are defined: N-glycolylneuraminic acid, NeuGc, is associated with type A and N-acetylneuraminic acid, NeuAc, with type B, overview
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
C1K3L2
-
-
-
?
CMP-N-acetylneuraminate + ferrocytochrome b5 + O2 + H+
CMP-N-glycoloylneuraminate + ferricytochrome b5 + H2O
-
-
-
-
ir
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
the enzyme is the key for regulation of the overall velocity of CMP-NeuAc hydroxylation and consequently for the expression of N-glycoloylneuraminic acid glycoconjugates
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
a regulation of CMP-N-acetylneuraminate hydroxylation and thus the ratio of glycoconjugate-bound N-acetylneuraminate and N-acetylglycoloylneuraminate might occur by varying the amount of hydroxylase protein within the cell, possibly by controlling the expression of the hydroxylase gene
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
the enzyme plays a decisive role in governing the relative amounts of N-acetylneuraminate and N-acetylglycolylneuraminate occuring in the glycoconjugates of a tissue
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
key enzyme for the expression of N-glycoloylneuraminic acid
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
-
-
-
?
CMP-N-acetylneuraminate + NADH + O2
CMP-N-glycoloylneuraminate + NAD+ + H2O
-
the biosynthesis of the sialic acid N-glycolylneuraminic acid occurs by the action of cytidine monophosphate-N-acetylneuraminate hydroxylase. Incorporation of N-glycoloylneuraminic acid into glycoconjugates is generally controlled by the amount of hydroxylase protein expressed in a tissue
-
-
?
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Lepers, A.; Shaw, L.; Schneckenburger, P.; Cacan, R.; Verbert, A.; Schauer, R.
A study on the regulation of N-glycoloylneuraminic acid biosynthesis and utilization in rat and mouse liver
Eur. J. Biochem.
193
715-723
1990
Mus musculus, Rattus norvegicus
brenda
Shaw, L.; Schauer, R.
The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid
Biol. Chem. Hoppe-Seyler
369
477-486
1988
Sus scrofa
brenda
Shaw, L.; Schauer, R.
Detection of CMP-N-acetylneuraminic acid hydroxylase activity in fractionated mouse liver
Biochem. J.
263
355-363
1989
Mus musculus
brenda
Kozutsumi, Y.; Kawano, T.; Yamakawa, T.; Suzuki, A.
Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol
J. Biochem.
108
704-706
1990
Mus musculus
brenda
Muchmore, E.A.; Milewski, M.; Varki, A.; Diaz, S.
Biosynthesis of N-glycolyneuraminic acid. The primary site of hydroxylation of N-acetylneuraminic acid is the cytosolic sugar nucleotide pool
J. Biol. Chem.
264
20216-20223
1989
Bos taurus, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Bergwerff, A.A.; Hulleman, S.H.D.; Kamerling, J.P.; Vliegenthart, J.F.G.; Shaw, L.; Reuter, G.; Schauer, R.
Nature and biosynthesis of sialic acids in the starfish Asterias rubens. Identification of sialo-oligomers and detection of S-adenosyl-L-methionine: N-acylneuraminate 8-O-methyltransferase and CMP-N-acetylneuraminate monooxygenase activities
Biochimie
74
25-37
1992
Asterias rubens
brenda
Schlenzka, W.; Shaw, L.; Kelm, S.; Schmidt, C.L.; Bill, E.; Trautwein, A.X.; Lottspeich, F.; Schauer, R.
CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulfur protein to be described in Eukarya
FEBS Lett.
385
197-200
1996
Sus scrofa
brenda
Shaw, L.; Schneckenburger, P.; Schlenzka, W.; Carlsen, J.; Christiansen, K.; Juergensen, D.; Schauer, R.
CMP-N-acetylneuraminic acid hydroxylase from mouse liver and pig submandibular glands. Interaction with membrane-bound and soluble cytochrome b5-dependent electron transport chains
Eur. J. Biochem.
219
1001-1011
1994
Bos taurus, Mus musculus, Sus scrofa
brenda
Martensen, I.; Schauer, R.; Shaw, L.
Cloning and expression of a membrane-bound CMP-N-acetylneuraminic acid hydroxylase from the starfish Asterias rubens
Eur. J. Biochem.
268
5157-5166
2001
Asterias rubens
brenda
Kawano, T.; Kozutsumi, Y.; Kawasaki, T.; Suzuki, A.
Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system
J. Biol. Chem.
269
9024-9029
1994
Mus musculus
brenda
Kawano, T.; Koyama, S.; Takematsu, H.; Kozutsumi, Y.; Kawasaki, H.; Kawashima, S.; Kawasaki, T.; Suzuki, A.
Molecular cloning of cytidine monophospho-N-acetylneuraminic acid hydroxylase. Regulation of species- and tissue-specific expression of N-glycolylneuraminic acid
J. Biol. Chem.
270
16458-16463
1995
Mus musculus
brenda
Chou, H.H.; Hayakawa, T.; Diaz, S.; Krings, M.; Indriati, E.; Leakey, M.; Paabo, S.; Satta, Y.; Takahata, N.; Varki, A.
Inactivation of CMP-N-acetylneuraminic acid hydroxylase occurred prior to brain expansion during human evolution
Proc. Natl. Acad. Sci. USA
99
11736-11741
2002
no activity in Homo sapiens
brenda
Irie, A.; Suzuki, A.
CMP-N-acetylneuraminic acid hydroxylase is exclusively inactive in humans
Biochem. Biophys. Res. Commun.
248
330-333
1998
Mus musculus, no activity in Homo sapiens
brenda
Schlenzka, W.; Shaw, L.; Schauer, R.
Catalytic properties of the CMP-N-acetylneuraminic acid hydroxylase from the starfish Asterias rubens: comparison with the mammalian enzyme
Biochim. Biophys. Acta
1161
131-138
1993
Asterias rubens
brenda
Takematsu, H.; Kawano, T.; Koyama, S.; Kozutsumi, Y.; Suzuki, A.; Kawasaki, T.
Reaction mechanism underlying CMP-N-acetylneuraminic acid hydroxylation in mouse liver: formation of a ternary complex of cytochrome b5, CMP-N-acetylneuraminic acid, and a hydroxylation enzyme
J. Biochem.
115
381-386
1994
Mus musculus
brenda
Schneckenburger, P.; Shaw, L.; Schauer, R.
Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver
Glycoconjugate J.
11
194-203
1994
Mus musculus
brenda
Koyama, S.; Yamaji, T.; Takematsu, H.; Kawano, T.; Kozutsumi, Y.; Suzuki, A.; Kawasaki, T.
A naturally occurring 46-amino acid deletion of cytidine monophospho-N-acetylneuraminic acid hydroxylase leads to a change in the intracellular distribution of the protein
Glycoconjugate J.
13
353-358
1996
Mus musculus
brenda
Malykh, Y.N.; Shaw, L.; Schauer, R.
The role of CMP-N-acetylneuraminic acid hydroxylase in determining the level of N-glycolylneuraminic acid in porcine tissues
Glycoconjugate J.
15
885-893
1998
Sus scrofa
brenda
Malykh, Y.N.; Krisch, B.; Shaw, L.; Warner, T.G.; Sinicrop, D.; Smith, R.; Chang, J.; Schauer, R.
Distribution and localization of CMP-N-acetylneuraminic acid hydroxylase and N-glycolylneuraminic acid-containing glycoconjugates in porcine lymph node and peripheral blood lymphocytes
Eur. J. Cell Biol.
80
48-58
2001
Sus scrofa
brenda
Gollub, M.; Schauer, R.; Shaw, L.
Cytidine monophosphate-N-acetylneuraminate hydroxylase in the starfish Asterias rubens and other echinoderms
Comp. Biochem. Physiol. B
120
605-615
1998
Asterias rubens, Ctenodiscus crispatus, Muelleria sp., Strongylocentrotus pallidus
brenda
Gollub, M.; Shaw, L.
Isolation and characterization of cytidine-5'-monophosphate-N-acetylneuraminate hydroxylase from the starfish Asterias rubens
Comp. Biochem. Physiol. B
134
89-101
2003
Asterias rubens
brenda
Schlenzka, W.; Shaw, L.; Schneckenburger, P.; Schauer, R.
Purification and characterization of CMP-N-acetylneuraminic acid hydroxylase from pig submandibular glands
Glycobiology
4
675-683
1994
Sus scrofa
brenda
Shaw, L.; Schneckenburger, P.; Carlsen, J.; Christiansen, K.; Schauer, R.
Mouse liver cytidine-5-monophosphate-N-acetylneuraminic acid hydroxylase. Catalytic function and regulation
Eur. J. Biochem.
206
269-277
1992
Mus musculus
brenda
Malykh, Y.N.; King, T.P.; Logan, E.; Kelly, D.; Schauer, R.; Shaw, L.
Regulation of N-glycolylneuraminic acid biosynthesis in developing pig small intestine
Biochem. J.
22
2-29
2002
Sus scrofa
-
brenda
Chenu, S.; Gregoire, A.; Malykh, Y.; Visvikis, A.; Monaco, L.; Shaw, L.; Schauer, R.; Marc, A.; Goergen, J.L.
Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in engineered Chinese hamster ovary cells using an antisense-RNA strategy
Biochim. Biophys. Acta
1622
133-144
2003
Cricetulus griseus
brenda
Malykh, Y.N.; Schauer, R.; Shaw, L.
N-Glycolylneuraminic acid in human tumours
Biochimie
83
623-634
2001
Homo sapiens
brenda
Hayakawa, T.; Aki, I.; Varki, A.; Satta, Y.; Takahata, N.
Fixation of the human-specific CMP-N-acetylneuraminic acid hydroxylase pseudogene and implications of haplotype diversity for human evolution
Genetics
172
1139-1146
2006
no activity in Homo sapiens
brenda
Bighignoli, B.; Niini, T.; Grahn, R.A.; Pedersen, N.C.; Millon, L.V.; Polli, M.; Longeri, M.; Lyons, L.A.
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Felis catus
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Schauer, R.; Srinivasan, G.V.; Coddeville, B.; Zanetta, J.P.; Guerardel, Y.
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no activity in Gallus gallus, no activity in Ornithorhynchus anatinus, no activity in Taeniopygia guttata
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Human CMP-N-acetylneuraminic acid hydroxylase (CMAH) is a novel stem cell marker linked to stem cell-specific mechanisms
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Homo sapiens (C1K3L2), Homo sapiens
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Sus scrofa (A8WAC5), Sus scrofa
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Mus musculus
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Mus musculus
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Bergfeld, A.; Pearce, O.; Diaz, S.; Pham, T.; Varki, A.
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Mus musculus
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Ikeda, K.; Yamamoto, A.; Nanjo, A.; Inuinaka, C.; Takama, Y.; Ueno, T.; Fukuzawa, M.; Nakano, K.; Matsunari, H.; Nagashima, H.; Miyagawa, S.
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Sus scrofa
brenda
Takahashi, T.; Kawagishi, S.; Funahashi, H.; Hayashi, N.; Suzuki, T.
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Chlorocebus aethiops, no activity in Homo sapiens
brenda
Gao, H.; Zhao, C.; Xiang, X.; Li, Y.; Zhao, Y.; Li, Z.; Pan, D.; Dai, Y.; Hara, H.; Cooper, D.K.; Cai, Z.; Mou, L.
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Sus scrofa
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Gandolfi, B.; Grahn, R.A.; Gustafson, N.A.; Proverbio, D.; Spada, E.; Adhikari, B.; Cheng, J.; Andrews, G.; Lyons, L.A.; Helps, C.R.
A novel variant in CMAH is associated with blood type AB in Ragdoll cats
PLoS ONE
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e0154973
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Felis catus
brenda
Omi, T.; Nakazawa, S.; Udagawa, C.; Tada, N.; Ochiai, K.; Chong, Y.H.; Kato, Y.; Mitsui, H.; Gin, A.; Oda, H.; Azakami, D.; Tamura, K.; Sako, T.; Inagaki, T.; Sakamoto, A.; Tsutsui, T.; Bonkobara, M.; Tsuchida, S.; Ikemoto, S.
Molecular characterization of the cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMAH) gene associated with the feline AB blood group system
PLoS ONE
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Felis catus (A6Y8N2), Felis catus
brenda
Sakai, R.; Esaki, Y.; Hasuwa, H.; Ikawa, M.; Lo, P.; Matsuura, R.; Nakahata, K.; Zenitani, M.; Asada, M.; Maeda, A.; Eguchi, H.; Okuyama, H.; Miyagawa, S.
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Sus scrofa (O19074), Sus scrofa
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