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hyaluronic acid tetrasaccharide + UDP-alpha-D-glucuronate
?
-
-
-
-
?
hyaluronic acid tetrasaccharide + UDP-alpha-N-acetyl-D-glucosamine
?
-
-
-
-
?
UDP-alpha-D-glucuronate + hyaluronan oligomer HA5
UDP + beta-D-glucuronosyl-(1->3)-hyaluronan oligomer HA5
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP-alpha-N-acetyl-D-glucosamine + hyaluronan oligomer HA4
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-hyaluronan oligomer HA4
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + hyaluronan oligomer HA6
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-hyaluronan oligomer HA6
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + hyaluronan oligomer HA8
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-hyaluronan oligomer HA8
-
-
-
?
UDP-D-glucosamine + UDP-D-glucuronate
[beta-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + n UDP
-
-
-
-
?
UDP-D-glucosamine + UDP-D-glucuronate
[beta-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-D-glucuronate + chondroitin 4-sulfate trisaccharide
?
-
3.6% of the activity with hyaluronan
-
-
?
UDP-D-glucuronate + chondroitin 6-sulfate pentasaccharide
?
-
61% of the activity with hyaluronan
-
-
?
UDP-D-glucuronate + chondroitin 6-sulfate trisaccharide
?
-
80% of the activity with hyaluronan
-
-
?
UDP-D-glucuronate + chondroitin sulfate
?
-
12% of the activity with hyaluronan
-
-
?
UDP-D-glucuronate + unsulfated chondroitin
?
-
54% of the activity with hyaluronan
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
[hyaluronan](n) + UDP-alpha-D-glucuronate
H+ + beta-D-glucuronosyl-(1->4)-[hyaluronan](n) + UDP
-
-
-
?
[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine
H+ + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP
-
-
-
?
additional information
?
-
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the linear heteropolysaccharide chain
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the linear heteropolysaccharide chain, recombinant isozyme HAS2 prefers the production of a mixture of 8mers and 16mers
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
chains growth at the non-reducing end, which is terminated by lack of substrate with a non-reducing end, active with exogenously added acceptors substrates
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
formation of linear hyaluronan polymers composed of alternating beta3-N-acetylglucosamine-beta4-glucuronic acid
the product chain length can grow at the reducing end up to 40000 monosaccharides with a MW of over 8 million Da before it is released by the class I enzyme
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
formation of linear hyaluronan polymers composed of alternating beta3-N-acetylglucosamine-beta4-glucuronic acid
the product chain length can grow at the reducing end up to 40000 monosaccharides with a MW of over 8 million Da before it is released by the class I enzyme
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
product is a linear chain
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the reducing end to form a linear heteropolysaccharide chain
product chain length depends on reaction conditions, overview
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
biosynthesis of hyaluronan
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the linear heteropolysaccharide chain composed of repeating disaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
highly specific for UDP-N-acetyl-D-glucosamine and UDP-D-glucuronate, addition of monosaccharides to the heteropolysaccharide chain consisting of repeated disaccharides up to 25000
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the reducing end to form a linear heteropolysaccharide chain
product chain length depends on reaction conditions, overview
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
biosynthesis of hyaluronan
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the reducing end of the acceptor substrate, no binding and activity with exogenously added hyaluronan chains
the product chain length can grow at the reducing end up to 40000 monosaccharides with a MW of over 8 million Da before it is released by the class I enzyme
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the linear heteropolysaccharide chain
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
additional information
?
-
-
hyaluronic acid synthase contributes to the pathogenesis of Cryptococcus neoformans infection
-
-
?
additional information
?
-
-
regulation mechanism of hyaluronan biosynthesis, stimulation of cells by cytokines effects the different expression patterns of the isoforms, especially during embryonic development, the isozymes have different roles in hyaluronan biosynthesis
-
-
?
additional information
?
-
-
the isozymes form products of different size, HA synthesis modeling, active site and substrate binding site are located on the big cytoplasmic loop
-
-
?
additional information
?
-
-
HAS2, localized in the plasma membrane, uses cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates
-
-
?
additional information
?
-
isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
-
-
?
additional information
?
-
isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
-
-
?
additional information
?
-
isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
-
-
?
additional information
?
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isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
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additional information
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two glycosyltransferase activities in HAS that add glucuronic acid and N-acetylglucosamine into their alternating positions in the chain, using UDP-glucuronic acid (UDP-GlcUA) and UDP-N-acetylglucosamine (UDP-GlcNAc) as substrates. Sufficient supply of both UDP-GlcUA and UDP-GlcNAc is important for hyaluronan synthesis
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additional information
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two glycosyltransferase activities in HAS that add glucuronic acid and N-acetylglucosamine into their alternating positions in the chain, using UDP-glucuronic acid (UDP-GlcUA) and UDP-N-acetylglucosamine (UDP-GlcNAc) as substrates. Sufficient supply of both UDP-GlcUA and UDP-GlcNAc is important for hyaluronan synthesis
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additional information
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two glycosyltransferase activities in HAS that add glucuronic acid and N-acetylglucosamine into their alternating positions in the chain, using UDP-glucuronic acid (UDP-GlcUA) and UDP-N-acetylglucosamine (UDP-GlcNAc) as substrates. Sufficient supply of both UDP-GlcUA and UDP-GlcNAc is important for hyaluronan synthesis
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additional information
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two glycosyltransferase activities in HAS that add glucuronic acid and N-acetylglucosamine into their alternating positions in the chain, using UDP-glucuronic acid (UDP-GlcUA) and UDP-N-acetylglucosamine (UDP-GlcNAc) as substrates. Sufficient supply of both UDP-GlcUA and UDP-GlcNAc is important for hyaluronan synthesis
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additional information
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a single protein exerts many functions as binding of two distinct UDP-sugars and binding of two distinct HA acceptor or donor species. The enzyme transfers two different sugars in two different linkages, catalyzes repetitive sugar polymerization, and transfers hyaluronan across the membrane
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additional information
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isozyme expression and regulation by interleukin-1beta, progesterone, and low-molecular-weight hyaluronan in pregnant mouse uterine cervix, overview
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additional information
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regulation mechanism of hyaluronan biosynthesis, stimulation of cells by cytokines effects the different expression patterns of the isoforms, especially during embryonic development, the isozymes have different roles in hyaluronan biosynthesis, isozymes exhibit different functions in tumor growth, progression, and determination of malignancy
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additional information
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the isozymes form products of different size, HA synthesis modeling, active site and substrate binding site are located on the big cytoplasmic loop
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additional information
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HA made by the has-1 transduced arterial smooth muscle cells is larger or part of a larger complex that resists proteolytic degradation when compared to the has-3 tansduced ASMCs. There is evidence that the different has enzymes have an inherent ability to regulate hyaluronan size
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additional information
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hyaluronan synthase 1 and hyaluronan synthase 2 synthesize high molecular weight hyaluronan, while hyaluronan synthase 3 synthesizes low lecular weight hyaluronan
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additional information
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hyaluronan synthase 1 and hyaluronan synthase 2 synthesize high molecular weight hyaluronan, while hyaluronan synthase 3 synthesizes low lecular weight hyaluronan
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additional information
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hyaluronan synthase 1 and hyaluronan synthase 2 synthesize high molecular weight hyaluronan, while hyaluronan synthase 3 synthesizes low lecular weight hyaluronan
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additional information
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enzyme is responsible for hyaluronan biosynthesis, the hyaluronan capsule is an important, but not the only, virulence factor, physiological role of the enzyme
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additional information
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the produced hyaluronan capsule enhances infection
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additional information
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enzyme is not processive, enzyme requires other proteins for hyaluronan translocation
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additional information
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substrate specificity, the GlcNAc-transferase, but not the GlcUA-transferase activity depends on the WGGED motif, overview
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additional information
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PmHAS elongates a range of acceptor molecules in addition to the cognate sugars. Certain glycosaminoglycans are very poor acceptors in comparison to the cognate molecules, but elongated products are detected. The interaction between the acceptor and the enzyme (a) the orientation of the hydroxyl at the C-4 position of the hexosamine is not critical, (b) the conformation of C-5 of the hexuronic acid (glucuronic versus iduronic) is not crucial, and (c) additional negative sulfate groups are well tolerated in certain cases, such as on C-6 of the hexosamine, but others, including C-4 sulfates, are not or are poorly tolerated
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additional information
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Pasteurella multocida hyaluronan synthase encompasses two transferase domains that elongate a growing hyaluronan oligosaccharide chain by addition of either GlcNAc or GlcUA residues from a corresponding UDP-sugar
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additional information
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a monodispersed hyaluronan chain can be obtained by finely tuning the reaction stoichiometry. The molar ratio of precursors and acceptor molecules has an important role in enzyme kinetics
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additional information
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initial velocity studies of single-step elongations are conducted for both domains by independently varying the concentrations of the hyaluronan oligosaccharide and the UDP-sugar. Two-substrate models are discriminated by their goodness-of-fit parameters and by dead-end inhibition studies. Coupled-enzyme assay using LDH, PK; NADH and phosphoenolpyruvate, as well as hyaluronan oligosaccharides, UDP-GlcNAc and UDP-GlcUA, overview
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additional information
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the produced hyaluronan capsule enhances infection
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additional information
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substrate specificity, the GlcNAc-transferase, but not the GlcUA-transferase activity depends on the WGGED motif, overview
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview, repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview, repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview, repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum
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additional information
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conserved cysteine residues are not essential for enzyme function
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additional information
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determination of polymer synthesis progression direction, overview
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additional information
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the enzyme is inactive without bound cardiolipins
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additional information
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a catalysis-transformation-translocation model is proposed for the hyaluronic acid synthesis and translocation processes. The residue R406 and R413 are primarily involved in catalysis, while the residues between 414 and 417 are involved in hyaluronic acid translocation
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additional information
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a catalysis-transformation-translocation model is proposed for the hyaluronic acid synthesis and translocation processes. The residue R406 and R413 are primarily involved in catalysis, while the residues between 414 and 417 are involved in hyaluronic acid translocation
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additional information
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the enzyme uses chitin-UDPs as primers to initiate hyaluronan synthesis, leaving the non-hyaluronan primer at the nonreducing end. chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the nonreducing-ends of hyaluronan chains as residual chitin
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additional information
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the enzyme uses chitin-UDPs as primers to initiate hyaluronan synthesis, leaving the non-hyaluronan primer at the nonreducing end. chitin-UDP functions in vitro and in live cells as a primer to initiate synthesis of all HA chains and these primers remain at the nonreducing-ends of hyaluronan chains as residual chitin
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additional information
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a three-dimensional atomic scale model of class I hyaluronan synthase enzymes is presented to gain insights on functional features. 9 hyaluronan synthase-specific sub-structural elements are identified. Docking studies with UDP-substrates in the enzyme show highly overlapping single binding sites for the two UDP-substrates. In-silico and mutation studies identify functional elements implicated in polymer binding and influencing hyaluronic acid production. The studies indicate a substrate binding role for Lys139, and a critical role for Gln248 and Thr283. Anisotropic Network Modeling (ANM)-based model is analysed to assess collective global dynamics in the enzyme. Based on ligand binding landscape and architecture of functional elements, a plausible three-step molecular mechanism to extend hyaluronic acid polymer from its reducing end is proposed. The release of UDP from polymeric end may be required for glycosyltransferase reaction
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additional information
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enzyme is responsible for hyaluronan biosynthesis, the hyaluronan capsule is an important, but not the only, virulence factor, physiological role of the enzyme
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additional information
?
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conserved cysteine residues are not essential for enzyme function
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additional information
?
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conserved cysteine residues are not essential for enzyme function
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additional information
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determination of polymer synthesis progression direction, overview
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additional information
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enzyme acts processive, the enzyme is active as a complex with cardiolipin, a bacterial membrane lipid
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additional information
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the substrate binding selectivity is more relaxed than the specificity of catalytic transfer, a nucleotide with 2 phosphate groups and complexed with a Mg2+ ion is absolutely required for activity
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UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
additional information
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UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
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-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
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-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-[nascent hyaluronan]
-
-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
-
-
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?
UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-[nascent hyaluronan]
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?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
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-
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?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
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-
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?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
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?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
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?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
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?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-(1-3)-N-acetyl-beta-D-glucosaminyl-(1-4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
?
UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan]
-
-
-
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the linear heteropolysaccharide chain
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
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?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the reducing end to form a linear heteropolysaccharide chain
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
biosynthesis of hyaluronan
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
-
addition of monosaccharides to the reducing end to form a linear heteropolysaccharide chain
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
biosynthesis of hyaluronan
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UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
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UDP-N-acetyl-D-glucosamine + UDP-D-glucuronate
[beta-N-acetyl-D-glucosaminyl(1-4)beta-D-glucuronosyl(1-3)]n + UDP
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additional information
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hyaluronic acid synthase contributes to the pathogenesis of Cryptococcus neoformans infection
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additional information
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regulation mechanism of hyaluronan biosynthesis, stimulation of cells by cytokines effects the different expression patterns of the isoforms, especially during embryonic development, the isozymes have different roles in hyaluronan biosynthesis
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additional information
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HAS2, localized in the plasma membrane, uses cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates
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additional information
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isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
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additional information
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isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
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additional information
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isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
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additional information
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isozyme HAS1 requires higher cellular UDP-GlcNAc concentration than isozymes HAS2 and HAS3. HAS1 is almost inactive in cells with low UDP-sugar supply, HAS2 activity increases with UDP-sugars, and HAS3 produces hyaluronan at high speed even with minimum substrate content. HAS works on the cytosolic pool of the UDPsugars
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additional information
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isozyme expression and regulation by interleukin-1beta, progesterone, and low-molecular-weight hyaluronan in pregnant mouse uterine cervix, overview
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additional information
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regulation mechanism of hyaluronan biosynthesis, stimulation of cells by cytokines effects the different expression patterns of the isoforms, especially during embryonic development, the isozymes have different roles in hyaluronan biosynthesis, isozymes exhibit different functions in tumor growth, progression, and determination of malignancy
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additional information
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HA made by the has-1 transduced arterial smooth muscle cells is larger or part of a larger complex that resists proteolytic degradation when compared to the has-3 tansduced ASMCs. There is evidence that the different has enzymes have an inherent ability to regulate hyaluronan size
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additional information
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enzyme is responsible for hyaluronan biosynthesis, the hyaluronan capsule is an important, but not the only, virulence factor, physiological role of the enzyme
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additional information
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the produced hyaluronan capsule enhances infection
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additional information
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Pasteurella multocida hyaluronan synthase encompasses two transferase domains that elongate a growing hyaluronan oligosaccharide chain by addition of either GlcNAc or GlcUA residues from a corresponding UDP-sugar
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additional information
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the produced hyaluronan capsule enhances infection
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview, repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview, repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum
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additional information
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isozyme expression and effects on tumor development and growth in rats, overview, repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum
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additional information
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enzyme is responsible for hyaluronan biosynthesis, the hyaluronan capsule is an important, but not the only, virulence factor, physiological role of the enzyme
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evolution
the three HAS isoenzymes, HAS1, HAS2, and HAS3, expressed in mammalian cells differ in their enzymatic properties and regulation by external stimuli
malfunction
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catalytically inactive mutant K190R HAS2 forms dimers with wild-type HAS2 and quenches the activity of wild-type HAS2
malfunction
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HAS-1 overexpression in dermal wounds decreases elements of scar formation
malfunction
reduction of HA due to decreased HAS activity, caused by phosphorylation at Thr110 through AMP-activated protein kinase, decreases the ability of aortic smooth muscle cells to proliferate, migrate, and recruit immune cells, thereby reducing the pro-atherosclerotic AoSMC phenotype. AMP-activated protein kinase can block the pro-atherosclerotic signals driven by HA by interaction with its receptors
malfunction
downregulation of HAS2 initiates and regulates fibroblast senescence through a p27-CDK2-SKP2 pathway. Deletion of HAS2 in mouse mesenchymal cells increases the cellular senescence of fibroblasts in bleomycin-induced mouse lung fibrosis in vivo. Overexpression of HAS2 in mesenchymal cells promotes an invasive phenotype resulting in severe fibrosis and downregulation of HAS2 promotes resolution. HAS2 deficiency leads to embryonic lethality. Downregulation of HAS2 increases p27 protein stability. p27 inhibits cell proliferation by regulating CDK2 activity. HAS2 deletion enhances cell stress responses. Phenotypes, detailed overview
malfunction
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embryonic lethality of genetic deletion of HAS2, some HAS2-specific functions are not compensated for by isozyme HAS1 or HAS3
malfunction
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in a ligation-induced carotid artery injury model, attenuated neointimal hyperplasia occurs in HAS3-null animals compared with wild-type control C57BL/6J mice. No changes are observed in medial and neointimal cell density, proliferation, or apoptosis. A lack of compensatory upregulation of isozymes HAS1 or HAS2, HAS3 deletion is associated with a reduction in vascular hyaluronan content, most dramatically in the media rather than the neointima. Transcriptome analysis of injured vessels from wild-type and HAS3-null mice reveals differential activation of pathways associated with a migratory VSMC phenotype. Isozyme HAS3 overexpression in VSMCs supports a migratory phenotype in response to platelet-derived growth factor BB (PDGF-BB), whereas knockdown of HAS3 results in reduced PDGF-BB-induced migration. Isozyme HAS3 knockdown also leads to a decrease in PDGF-B mRNA levels
malfunction
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isozyme HAS3 overexpression downregulates MV3 melanoma cell proliferation, migration and adhesion. Overexpression of isozyme HAS3 decreases cell proliferation, directional and random cell migration, and promotes cell cycle arrest at G1/G0 and decreases ERK1/2 phosphorylation suggesting that inhibition of MAP-kinase signaling is responsible for the suppressive effects on the malignant phenotype of MV3 melanoma cells. EGFP-HAS3 overexpression downregulates several signaling pathways in MV3 melanoma cells
malfunction
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the regulation of isozyme HAS2 by O-GlcNAcylation can have important therapeutic consequences considering that the excess of glucose can lead to a dramatic increase of UDP-GlcNAc and hyaluronan (in particular in cells where the uptake of glucose is insulin-independent). Clinical and experimental evidences show that in hyperglycemic patients and in streptozotocin-induced diabetes animals there is evidence of hyaluronan accumulation both in plasma and in vascular wall
malfunction
Has2-/- mice are embryonic lethal. Has2-/- embryos die between embryonic day 9.5 and 10.5 and exhibit severe cardiac and vascular abnormalities, in addition to yolk sac and somite deformities
malfunction
Has3/Apoe double deficient mice develop less atherosclerosis characterized by decreased Th1-cell responses, decreased IL-12 release, and decreased macrophage-driven inflammation
malfunction
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in a ligation-induced carotid artery injury model, attenuated neointimal hyperplasia occurs in HAS3-null animals compared with wild-type control C57BL/6J mice. No changes are observed in medial and neointimal cell density, proliferation, or apoptosis. A lack of compensatory upregulation of isozymes HAS1 or HAS2, HAS3 deletion is associated with a reduction in vascular hyaluronan content, most dramatically in the media rather than the neointima. Transcriptome analysis of injured vessels from wild-type and HAS3-null mice reveals differential activation of pathways associated with a migratory VSMC phenotype. Isozyme HAS3 overexpression in VSMCs supports a migratory phenotype in response to platelet-derived growth factor BB (PDGF-BB), whereas knockdown of HAS3 results in reduced PDGF-BB-induced migration. Isozyme HAS3 knockdown also leads to a decrease in PDGF-B mRNA levels
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malfunction
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HAS-1 overexpression in dermal wounds decreases elements of scar formation
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metabolism
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regulation of hexosamine biosynthetic pathway, biosynthesis of hyaluronan and other glycoconjugates, and protein O-GlcNAcylation, overview
metabolism
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role of hyaluronan in vascular disease, a multitude of synthases (HAS1, HAS2, and HAS3) and multiple hyaluronidases are involved in its metabolism
metabolism
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role of hyaluronan in vascular disease, a multitude of synthases (HAS1, HAS2, and HAS3) and multiple hyaluronidases are involved in its metabolism
metabolism
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the most general sensor of cellular nutritional status is the hexosamine biosynthetic pathway that brings to the formation of UDP-GlcNAc and intracellular protein glycosylation by O-linked attachment of the monosaccharide beta-N-acetylglucosamine (O-GlcNAcylation) to specific aminoacid residues. Such highly dynamic and ubiquitous protein modification affects residue Ser221 residue of isozyme HAS2 that lead to a dramatic stabilization of the enzyme in the membrane
metabolism
histamine controls hyaluronan metabolism by up-regulating HYBID (hyaluronan-binding protein) and down-regulating hyaluronan synthase 2 (HAS2) via distinct signaling pathways downstream of histamine receptor H1
metabolism
hyaluronan is expressed in a temporal-spatial expression pattern and may play a role in embryonic tooth morphogenesis. The difference in the distribution and expression of the three hyaluronan synthases at different developmental stages also supports their roles in cell proliferation, cell differentiation and cell migration
metabolism
hyaluronan synthase 2 expression is elevated in both human and murine liver fibrosis. The enzyme actively synthesizes hyaluronan in hepatic stellate cells and promotes activation of hepatic stellate cells and liver fibrosis through Notch1
metabolism
hyaluronan synthase 2 expression is elevated in both human and murine liver fibrosis. The enzyme actively synthesizes hyaluronan in hepatic stellate cells and promotes activation of hepatic stellate cells and liver fibrosis through Notch1
metabolism
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role of hyaluronan in vascular disease, a multitude of synthases (HAS1, HAS2, and HAS3) and multiple hyaluronidases are involved in its metabolism
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physiological function
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hyaluronan concentration in follicular fluids increases during atresia. Isoform HAS1 may be the dominant HAS protein in theca cells to produce hyaluronan in pig ovaries
physiological function
inhibition of HAS2 expression by siRNA decreases matrix metalloprotein MMP-7 expression by about 20%, and dramaticlly decreases MMP-7 protein, and enzymatic activity. HAS isoforms and hyaluronan may mediate cellular invasion via changes in matrix metalloprotein MMP-7 expression
physiological function
inhibition of HAS2 expression by siRNA decreases matrix metalloprotein MMP-7 expression by about 30%, and dramaticlly decreases MMP-7 protein, and enzymatic activity. HAS isoforms and hyaluronan may mediate cellular invasion via changes in matrix metalloprotein MMP-7 expression
physiological function
mainly high molecular weight hyaluronan synthesized by isoform HAS1 regulates HT-1080 cell motility
physiological function
the reduction of hyaluronan caused by enzyme downregulation through 4-methylumbelliferone is associated with a significant inhibition of cell migration, proliferation and invasion
physiological function
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HAS-1 treatment of wounds promotes a more organized extracellular matrix with the regeneration of dermal appendages, including hair follicles, increased regenerative healing, overview
physiological function
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hyaluronan synthase mediates dye translocation across liposomal membranes
physiological function
hyaluronan synthesis is inhibited by adenosine monophosphate-activated protein kinase through the regulation of HAS2 activity in human aortic smooth muscle cells
physiological function
the expression of the Has1 isoenzyme, most dependent on high UDP-sugar contents, is coordinated with a metabolic state that maintains a high level of these substrates
physiological function
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the hyaluronan synthase catalyzes the synthesis and membrane translocation of hyaluronan, it is both necessary and sufficient to translocate hyaluronan in a reaction that is tightly coupled to hyaluronan elongation. Hyaluronan synthesis and translocation are spatially coupled events, which allow hyaluronan synthesis even in the presence of a large excess of hyaluronan-degrading enzyme
physiological function
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the role of UDP-N-acetylglucosamine and O-GlcNAc-acylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis, overview. O-linked GlcNAc (O-GlcNAcylation) is regulated by the action of two enzymes, O-GlcNAc transferase and O-GlcNAc hydrolase. The HA increase due to O-GlcNAcylation regulates inflammatory cell adhesion, the number of monocytes that adhere on AoSMC monolayer cultures is increased
physiological function
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hyaluronan is a glycosaminoglycan composed by repeating units of D-glucuronic acid and N-acetylglucosamine that is ubiquitously present in the extracellular matrix where it has a critical role in the physiology and pathology of several mammalian tissues. Hyaluronan represents a perfect environment in which cells can migrate and proliferate. Several receptors can interact with hyaluronan at cellular level triggering multiple signal transduction responses. The control of the hyaluronan synthesis is therefore critical in extracellular matrix assembly and cell biology, analysis of metabolic regulation of hyaluronan synthesis, overview. In contrast with other glycosaminoglycans, which are synthesized in the Golgi apparatus, hyaluronan is produced at the plasma membrane by hyaluronan synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates. UDP-GlcUA and UDP-hexosamine availability is critical for the synthesis of glycosaminoglycans, an energy consuming process
physiological function
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hyaluronan is a ubiquitous glycosaminoglycan involved in embryonic development, inflammation and cancer. In mammals, three hyaluronan synthase isoenzymes (HAS1-3) inserted in the plasma membrane produce hyaluronan directly on the cell surface. Isozyme hyaluronan synthase 1 (HAS1) produces a cytokine-and glucose-inducible, CD44-dependent cell surface coat
physiological function
hyaluronan is the largest and one of the most abundant glycosaminoglycans of the extracellular space. Hyaluronan synthases are glycosyltransferases acting on the inner face of plasma membrane, adding alternately glucuronic acid and N-acetylglucosamine to the reducing end of the growing chain. Hyaluronan synthase forms a reserve that is transported to the plasma membrane for rapid activation of hyaluronan synthesis. The levels and localizations of HAS isoforms are likely to be highly important in processes like embryonic development, wound healing, inflammation, and malignant growth
physiological function
hyaluronan synthase 1 (HAS1) is one of three isoenzymes responsible for cellular hyaluronan synthesis. The role of HAS1 in hyaluronan production seems to be insignificant compared to the two other isoenzymes, HAS2 and HAS3, which have higher enzymatic activity. Isozyme Has1 is upregulated in states associated with inflammation, like atherosclerosis, osteoarthritis, and infectious lung disease. Both full length and splice variants of HAS1 are expressed in malignancies like bladder and prostate cancers, multiple myeloma, and malignant mesothelioma. The pericellular hyaluronan coat produced by HAS1 is usually thin without induction by inflammatory agents or glycemic stress and depends on CD44HA interactions. These specific interactions regulate the organization of hyaluronan into a leukocyte recruiting matrix during inflammatory responses. Despite the apparently minor enzymatic activity of HAS1 under normal conditions, it may be an important factor under conditions associated with glycemic stress like metabolic syndrome, inflammation, and cancer. HAS1 expression is transcriptionally regulated by transforming growth factor-beta in synoviocytes and by the pro-inflammatory cytokine interleukin-1beta in fibroblasts, while these factors may have similar or opposite effects on other HASs, depending on the cell type. Has1 is associated with breast tumor and with estrogen receptor negativity, HER2 positivity, high relapse rate, and short overall survival
physiological function
hyaluronan synthase 2 regulates fibroblast senescence in pulmonary fibrosis. Senescence is implicated in development, cancer, and tissue fibrosis. The chronic inflammation caused by cellular senescence may be related to the pathogenesis of various chronic diseases. Isozyme HAS2 may be a critical regulator of the fate of pulmonary fibrosis. Isozyme HAS2 is the major isoform responsible for hyaluronan production in mesenchymal cells
physiological function
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hyaluronan synthase isozymes are involved in hyaluronan biosynthesis. Each HAS isoform produces structurally identical hyaluronan, thus, hyaluronan function is independent of the HAS by which it is synthesized. Hyaluronan is an essential component of the pericellular matrix, or alternatively, it can be released in a soluble form and be released and incorporated as part of the extracellular matrix. The composition and architecture of the matrix affect hyaluronan-dependent biochemical signaling, as well as the biophysical and biomechanical properties of tissues. The temporal and spatial relationship of hyaluronan with cells that express hyaluronidases that modify the molecular weight of hyaluronan is another determinant of hyaluronan function. Hyaluronan synthases may affect vascular disease independent of hyaluronan. HAS isoform-specific functions in tissue homeostasis and disease
physiological function
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hyaluronan synthase isozymes are involved in hyaluronan biosynthesis. Each HAS isoform produces structurally identical hyaluronan, thus, hyaluronan function is independent of the HAS by which it is synthesized. Hyaluronan is an essential component of the pericellular matrix, or alternatively, it can be released in a soluble form and be released and incorporated as part of the extracellular matrix. The composition and architecture of the matrix affect hyaluronan-dependent biochemical signaling, as well as the biophysical and biomechanical properties of tissues. The temporal and spatial relationship of hyaluronan with cells that express hyaluronidases that modify the molecular weight of hyaluronan is another determinant of hyaluronan function. Hyaluronan synthases may affect vascular disease independent of hyaluronan. HAS isoform-specific functions in tissue homeostasis and disease. Apotential autocrine loop involving isoyzme HAS3, PDGF-B expression, and PDGF-BB-induced migration. Isoform-specific role for HAS3 in promoting neointimal hyperplasia after carotid artery ligation
physiological function
recombinant hyaluronan synthase-2 upregulation protects smpd3-deficient fibroblasts against cell death induced by nutrient deprivation, but not against apoptosis evoked by human oxidized LDL. Resistance of fro/fro cells to starvation-induced apoptosis is associated with an increased expression of hyaluronan synthase 2 (HAS2) mRNAs and protein, which is inhibited by ceramide. The protective mechanism of HAS2 involves an increased expression of the heat-shock protein Hsp72, a chaperone with antiapoptotic activity. Antiapoptotic properties of HAS2 , overview
physiological function
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the enzyme is involved in synthesis of hyaluronan that may have anti-cancer like effects in melanoma progression
physiological function
enzyme expression has a pivotal role in cell motility and invasion. The enzyme regulates tumor progression and cell aggressiveness. Mammary tumor biopsies in which the enzyme (HAS2) is overexpressed display enhanced angiogenesis and inflammatory cells recruitment. HAS2 is a critical factor that induces epithelial-mesenchymal transition
physiological function
hyaluronan synthase 3 promotes plaque inflammation and atheroprogression. Hyaluronan synthase 3 expression in vascular smooth muscle cells is found to be regulated by interleukin 1 beta (IL-1beta) in an NFkappaB dependent manner
physiological function
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recombinant hyaluronan synthase-2 upregulation protects smpd3-deficient fibroblasts against cell death induced by nutrient deprivation, but not against apoptosis evoked by human oxidized LDL. Resistance of fro/fro cells to starvation-induced apoptosis is associated with an increased expression of hyaluronan synthase 2 (HAS2) mRNAs and protein, which is inhibited by ceramide. The protective mechanism of HAS2 involves an increased expression of the heat-shock protein Hsp72, a chaperone with antiapoptotic activity. Antiapoptotic properties of HAS2 , overview
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physiological function
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hyaluronan synthase isozymes are involved in hyaluronan biosynthesis. Each HAS isoform produces structurally identical hyaluronan, thus, hyaluronan function is independent of the HAS by which it is synthesized. Hyaluronan is an essential component of the pericellular matrix, or alternatively, it can be released in a soluble form and be released and incorporated as part of the extracellular matrix. The composition and architecture of the matrix affect hyaluronan-dependent biochemical signaling, as well as the biophysical and biomechanical properties of tissues. The temporal and spatial relationship of hyaluronan with cells that express hyaluronidases that modify the molecular weight of hyaluronan is another determinant of hyaluronan function. Hyaluronan synthases may affect vascular disease independent of hyaluronan. HAS isoform-specific functions in tissue homeostasis and disease. Apotential autocrine loop involving isoyzme HAS3, PDGF-B expression, and PDGF-BB-induced migration. Isoform-specific role for HAS3 in promoting neointimal hyperplasia after carotid artery ligation
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physiological function
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HAS-1 treatment of wounds promotes a more organized extracellular matrix with the regeneration of dermal appendages, including hair follicles, increased regenerative healing, overview
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additional information
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HA product size is decreased by increasing concentrations of glycerol. The four Cys residues in SeHAS are clustered close together and are located at the membrane-HAS interface within the enzyme active site. Involvement of these Cys residues in HAS activity, overview
additional information
product hyaluronan is secreted to the cell surface or the into the growth medium by HAS-containing cell culture, respectively
additional information
product hyaluronan is secreted to the cell surface or the into the growth medium by HAS-containing cell culture, respectively
additional information
product hyaluronan is secreted to the cell surface or the into the growth medium by HAS-containing cell culture, respectively
additional information
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product hyaluronan is secreted to the cell surface or the into the growth medium by HAS-containing cell culture, respectively
additional information
An important factor affecting activity of all HAS enzymes is the cytoplasmic availability of substrates, namely, UDP-GlcUA and UDP-GlcNAc. This role of substrates is particularly interesting in regulation of HAS1 as its activity of hyaluronan production in many cell models is low or absent unless stimulated
additional information
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the mechanism of HAS2 proteasomal degradation is complex and requires additional processes considering the several transmembrane domains of HAS2 and its localization in the plasma membrane
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S221A
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site-directed mutation of the O-GlcNAcylable Ser-221 to alanine generated an enzyme with a calculated t1/2 of about 70 min
T110A
site-directed mutagenesis of the phosphorylation site residue, the mutant is not inhibited by AMP-activated protein kinase
D216A
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site-directed mutagenesis, isozyme HAS3, inactive mutant
K190R
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site-directed mutagenesis, inactive mutant, K190R-mutated HAS2 forms dimers with wild-type HAS2 and quenches the activity of wild-type HAS2
D196N
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mutants possess UDP-D-glucuronate-transferase activity
D247E
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D247K
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D247N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D249E
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D249K
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D249N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D370E
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low hyaluronan synthase activity
D370K
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
D370N
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
D477K
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mutants possess UDP-N-acetyl-D-glucosamine-transferase activity
D527E
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
D527K
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
D527N
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
D529E
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site-directed mutagenesis, mutant possesses GlcNAc-transferase activity, and low hyaluronan synthase activity
D529K
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site-directed mutagenesis, mutant possesses GlcNAc-transferase activity, and very low hyaluronan synthase activity
D529N
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
E369D
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
E369H
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
E369Q
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
D247E
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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D247K
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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D247N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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D249N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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C226A/C262A/C367A
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site-directed mutagenesis, 1.4% remaining activity and altered kinetic constants compared to the wild-type enzyme
delD409-L417
deletion of 409-DWGTRKKLL-417 causes significant decreases in hyaluronic acid titer and in vitro hyaluronan synthase activity and undetectable hyaluronic acid weight-average molecular weight. Stepping truncations from L417 to K415 have little impact on hyaluronic acid and molecular weight. The removal of L417-K414, the hyaluronic acid titer of the resulting WGTR413 variant dramatically decreased to 16.8% of the wild type, while the same hyaluronic acid molecular weight is still detectable. With the further removal of R413, the hyaluronic acid titer of the resulting WGT412 variant dropps to less than 10% of the wild-type, and no hyaluronic acid products are detectable
E327D
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the specific enzyme activity relative to wild type enzyme is 38%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
E327K
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the specific enzyme activity relative to wild type enzyme is 0.16%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
E327K/K48E
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the specific enzyme activity near wild-type level. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzymel
E327Q
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the specific enzyme activity relative to wild type enzyme is 26%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
K414A
mutation does not notably affect hyaluronic acid titer
K414R
mutation does not notably affect hyaluronic acid titer. The molecular weight of the hyaluronic acid produced by the K414R variant is significantly increased
K415A
mutation does not notably affect hyaluronic acid titer
K415R
mutation does not notably affect hyaluronic acid titer
K48F
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site-directed mutagenesis, alteration of K48 within membrane domain 2 causes decreased activity and HA product size
K48R
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the specific enzyme activity relative to wild type enzyme is 17%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
R406A
hyaluronic acid titer is greatly decreased
R413A
hyaluronic acid titer is greatly decreased
R413K
the variant barely produces hyaluronic acid
T412A
mutations completely deactivates the enzyme
W410A
mutations completely deactivates the enzyme
N196I/L197R/T202S/D203H/C226F/S231D/V232F/E236Q/S256N/C262S/K294T/N297H/N300K/F303C
the enzyme is engineered to increase hyaluronan production and molecular mass through structural alteration of multiple regions. As compared with other variants and wild-type enzyme, the V5 variant generates a higher hyaluronan titer (2.24 g/l) and molecular weight value (1360000 Da). Following overexpression of the genes tuaD and glmU in Bacillus subtilis V5, hyaluronan production and molecular weight increases further to 2.81 g/l and 2430000 Da, respectively. The results provide a new strategy for producing hyaluronan with higher titers and molecular mass values that could be extended to other polysaccharides, such as heparosan and chondroitin, produced in Bacillus subtilis
C117F
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site-directed mutagenesis, no expression in yeast possible
C117L
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C117S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C210S
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C239S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C239S/C337S
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site-directed mutagenesis, reduced recombinant expression level, activity is similar to the wild-type enzyme
C298F
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site-directed mutagenesis, poor recombinant expression level, highly reduced activity compared to the wild-type enzyme
C298L
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site-directed mutagenesis, poor recombinant expression level, highly reduced activity compared to the wild-type enzyme
C298S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C304S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C304S/C337S
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C307S
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C307S/C337S
-
site-directed mutagenesis, reduced recombinant expression level, inactive mutant
C337S
-
site-directed mutagenesis, increased Km for UDP-N-acetylglucosamine compared to the wild-type enzyme
C226A
-
site-directed mutagenesis, 24% remaining activity and altered kinetic constants compared to the wild-type enzyme
C226A
-
site-directed mutagenesis, increased sensitivity to inhibition by NEM
C226A
-
site-directed mutagenesis, the mutant shows 44% of wild-type activity
C226A/C262A
-
site-directed mutagenesis, 3.2% remaining activity and altered kinetic constants compared to the wild-type enzyme
C226A/C262A
-
site-directed mutagenesis, slightly increased sensitivity to inhibition by NEM, and reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C226A/C262A
-
site-directed mutagenesis, the mutant shows 36% of wild-type activity, mutant kinetics compared to the wild-type enzyme
C226A/C281A
-
site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C226A/C281A
-
site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C226A/C281A
-
site-directed mutagenesis, the mutant shows 68% of wild-type activity
C226A/C367A
-
site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C226A/C367A
-
site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and slightly increased sensitivity to inhibition by sodium arsenite compared to the wild-type
C226A/C367A
-
site-directed mutagenesis, the mutant shows 102% of wild-type activity
C226S
-
site-directed mutagenesis, highly reduced reaction velocity and altered Km values compared to the wild-type enzyme
C226S
-
site-directed mutagenesis, reduced sensitivity to inhibition by NEM
C226S
-
site-directed mutagenesis, the mutant shows 45% of wild-type activity, mutant kinetics compared to the wild-type enzyme
C262A
-
site-directed mutagenesis, increased sensitivity to inhibition by NEM
C262A
-
site-directed mutagenesis, reduced reaction velocity and increased Km values compared to the wild-type enzyme
C262A
-
site-directed mutagenesis, the mutant shows 79% of wild-type activity
C262A/C281A
-
site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C262A/C281A
-
site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C262A/C281A
-
site-directed mutagenesis, the mutant shows 82% of wild-type activity, mutant kinetics compared to the wild-type enzyme
C262A/C367A
-
site-directed mutagenesis, increased sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C262A/C367A
-
site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C262S
-
site-directed mutagenesis, increased sensitivity to inhibition by NEM
C262S
-
site-directed mutagenesis, reduced reaction velocity and increased Km values compared to the wild-type enzyme
C262S
-
site-directed mutagenesis, the mutant shows 85% of wild-type activity
C281A
-
site-directed mutagenesis, highly reduced sensitivity to inhibition by NEM
C281A
-
site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C281A
-
site-directed mutagenesis, the mutant shows 91% of wild-type activity
C281A/C367A
-
site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C281A/C367A
-
site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C281A/C367A
-
site-directed mutagenesis, the mutant shows 107% of wild-type activity
C281S
-
site-directed mutagenesis, increased sensitivity to inhibition by NEM
C281S
-
site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C281S
-
site-directed mutagenesis, the mutant shows 57% of wild-type activity
C367A
-
site-directed mutagenesis, increased reaction velocity and Km values compared to the wild-type enzyme
C367A
-
site-directed mutagenesis, unaltered inhibition by NEM compared to the wild-type enzyme
C367A
-
site-directed mutagenesis, the mutant shows 126% of wild-type activity
C367S
-
site-directed mutagenesis, kinetics similar to the wild-type enzyme
C367S
-
site-directed mutagenesis, unaltered inhibition by NEM compared to the wild-type enzyme
C367S
-
site-directed mutagenesis, the mutant shows 80% of wild-type activity
K48E
-
the specific enzyme activity relative to wild type enzyme is 7%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
K48E
-
site-directed mutagenesis, alteration of K48 within membrane domain 2 causes decreased activity and HA product size
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
-
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
-
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
-
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
both COS-1 and MCF-7 cell lines have negligible endogenous hyaluronan production, and even overexpression of HAS1 enzymes does not cause prominent changes in it. Upon treatment with glucose or glucosamine, compounds that increase the amounts of hyaluronan substrates, the HAS1 enzyme is able to produce significant amounts of hyaluronan
additional information
-
HAS1-transfected MCF-7cells show very little cell surface hyaluronan, but a large hyaluronan coat is seen in cells grown in 20 mM glucose and 1 mM glucosamine, or treated with interleukin-1beta, TNF-alpha, or TGF-beta. The coats are mostly removed by the presence of hyaluronan hexasaccharides, or Hermes1 antibody, indicating that they depend on the CD44 receptor, which is, in contrast to the coat produced by HAS3, remaining attached to HAS3 itself
additional information
-
isozyme HAS3 overexpression expands the cell surface hyaluronan coat and decreases melanoma cell adhesion, migration and proliferation by cell cycle arrest at G1/G0. Melanoma cell migration is restored by removal of cell surface hyaluronan by Streptomyces hyaluronidase and by receptor blocking with hyaluronan oligosaccharides, while the effect on cell proliferation is receptor independent. Overexpression of isozyme HAS3 decreases ERK1/2 phosphorylation suggesting that inhibition of MAP-kinase signaling is responsible for the suppressive effects on the malignant phenotype of MV3 melanoma cells
additional information
-
construction of deletion mutants of isozyme HAS3
additional information
-
site-directed mutagenesis of residues of the cytoplasmic loop of isozyme HAS1 for determining the residues required for glycosyltransferase activity
additional information
enzyme downregulation by HAS2 siRNA transfection
additional information
-
enzyme downregulation by HAS2 siRNA transfection
additional information
-
activity rescue of mutants with high substrate concentrations, overview, deletion of residues 1-117 does not affect polymerization activity, construction of different chimeric mutant enzymes comprising residues from Pasteurella multocida type A enzyme and residues of a Pasteurella multocida type F chondroitin synthase, producing an unsulfated chondroitin capsule, the chimeric mutants show different percentages of hyaluronan and chondroitin synthase ativities, overview
additional information
-
a truncated soluble form of recombinant PmHAS (residues 1703) can catalyze the glycosyl transfers in a time- and concentration-dependent manner
additional information
-
activity rescue of mutants with high substrate concentrations, overview, deletion of residues 1-117 does not affect polymerization activity, construction of different chimeric mutant enzymes comprising residues from Pasteurella multocida type A enzyme and residues of a Pasteurella multocida type F chondroitin synthase, producing an unsulfated chondroitin capsule, the chimeric mutants show different percentages of hyaluronan and chondroitin synthase ativities, overview
-
additional information
expression of isozyme HAS1 is increased after oncogenic malignant transformation with v-sre and/or v-fos, no increase after transformation with v-HA-ras, introduction of isozyme HAS1 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS1 is increased after oncogenic malignant transformation with v-sre and/or v-fos, no increase after transformation with v-HA-ras, introduction of isozyme HAS1 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS1 is increased after oncogenic malignant transformation with v-sre and/or v-fos, no increase after transformation with v-HA-ras, introduction of isozyme HAS1 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS2 is increased after oncogenic malignant transformation with v-HA-ras, v-sre and/or v-fos, antisense repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum, introduction of isozyme HAS2 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS2 is increased after oncogenic malignant transformation with v-HA-ras, v-sre and/or v-fos, antisense repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum, introduction of isozyme HAS2 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS2 is increased after oncogenic malignant transformation with v-HA-ras, v-sre and/or v-fos, antisense repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum, introduction of isozyme HAS2 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
-
construction and kinetic analysis of Cys-deletion mutants, overview
additional information
-
construction of cysteine-deletion mutants deleting either C226, C262, C281, or C367, the mutants are less sensitive or not sensisitive to sodium arsenite inhibition, overview
additional information
-
addition of purified HAS to liposomes preloaded with the fluorophore Cascade Blue, CB, which is translocated through the membrane and secreted by HAS, overview. SeHAS-mediated CB efflux is greater from liposomes made with an activating lipid, tetraoleoyl cardiolipin, compared to an inactivating lipid, tetramyristoyl cardiolipin
additional information
-
generation of several deletion mutants, DELTA3-C281, DELTA3-C226, DELTA3-C262, and DELTA3-C367, and of a C-null mutant, all show reduced activity and altered kinetics compared to the wild-type enzyme
additional information
-
purified Se-HAS is reconstituted into proteoliposomes, from total lipid extract from Escherichia coli, where it synthesizes and translocates hyaluronan, or reconstituted into synthetic 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine/1,1',2,2'-tetraoleoyl cardiolipin/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (80/10/10%) proteoliposomes. In vitro synthesized, high-molecular-weight hyaluronan remains tightly associated with the intact proteoliposomes, even after proteolyticdegradation of HAS or in the presence of 1 M NaCl or 0.6 M urea to prevent nonspecific interactions of the polymer with the lipid vesicles
additional information
-
dual expression of hyaluronan synthase and UDP-glucose-6-dehydrogenase in Lactococcus lactis and study of the ratios of hyaluronan synthase expression level to the precursor sugar UDP-GlcA biosynthesis ability under different induction concentration collocations with nisin and lactose on the molecular weight of hyaluronan. The final weight-average molecular weight of hyaluronan correlates with the relative ratios of hyaluronan synthase expression level to the concentration of UDP-GlcA
additional information
-
dual expression of hyaluronan synthase and UDP-glucose-6-dehydrogenase in Lactococcus lactis and study of the ratios of hyaluronan synthase expression level to the precursor sugar UDP-GlcA biosynthesis ability under different induction concentration collocations with nisin and lactose on the molecular weight of hyaluronan. The final weight-average molecular weight of hyaluronan correlates with the relative ratios of hyaluronan synthase expression level to the concentration of UDP-GlcA
-
additional information
-
variety of cystein mutatants
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DeAngelis, P.L.; Papaconstantinou, J.; Weigel, P.H.
Molecular cloning, identification and sequence of the hyaluronan synthase gene from Group A Streptococcus pyogenes
J. Biol. Chem.
268
19181-19184
1993
Streptococcus pyogenes
brenda
DeAngelis, P.L.; Weigel, P.H.
Immunochemical confirmation of the primary structure of streptococcal hyaluronan synthase and synthesis of high molecular weight product by the recombinant enzyme
Biochemistry
33
9033-9039
1994
Streptococcus pyogenes
brenda
Spicer, A.P.; Augustine, M.L.; McDonald, J.A.
Molecular cloning and characterization of a putative mouse hyaluronan synthase
J. Biol. Chem.
271
23400-23406
1996
Mus musculus (P70312), Mus musculus
brenda
Kumari, K.; Weigel, P.H.
Molecular cloning, expression, and characterization of the authentic hyaluronan synthase from group C Streptococcus equisimilis
J. Biol. Chem.
272
32539-32546
1997
Streptococcus dysgalactiae subsp. equisimilis
brenda
DeAngelis, P.L.; Jing, W.; Graves, M.V.; Burbank, D.E.; Van Etten, J.L.
Hyaluronan synthase of chlorella virus PBCV-1
Science
278
1800-1803
1997
Paramecium bursaria Chlorella virus 1
brenda
Itano, N.; Sawai, T.; Yoshida, M.; Lenas, P.; Yamada, Y.; Imagawa, M.; Shinomura, T.; Hamaguchi, M.; Yoshida, Y.; Ohnuki, Y.; Miyauchi, S.; Spicer, A.P.; McDonald, J.A.; Kimata, K.
Three isoforms of mammalian hyaluronan synthases have distinct enzymatic properties
J. Biol. Chem.
274
25085-25092
1999
Mus musculus
brenda
Pummill, P.E.; Achyuthan, A.M.; DeAngelis, P.L.
Enzymological characterization of recombinant Xenopus DG42, a vertebrate hyaluronan synthase
J. Biol. Chem.
273
4976-4981
1998
Xenopus laevis, Xenopus laevis protein DG42
brenda
Tlapak-Simmons, V.L.; Baggenstoss, B.A.; Clyne, T.; Weigel, P.H.
Purification and lipid dependence of the recombinant hyaluronan synthases from Streptococcus pyogenes and Streptococcus equisimilis
J. Biol. Chem.
274
4239-4245
1999
Streptococcus dysgalactiae subsp. equisimilis, Streptococcus pyogenes
brenda
DeAngelis, P.L.
Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase
J. Biol. Chem.
274
26557-26562
1999
Pasteurella multocida (Q7BLV3), Pasteurella multocida
brenda
Jing, W.; DeAngelis, P.L.
Dissection of the two transferase activities of the Pasteurella multocida hyaluronan synthase: two active sites exist in one polypeptide
Glycobiology
10
883-889
2000
Pasteurella multocida
brenda
Heldermon, C.D.; Tlapak-Simmons, V.L.; Baggenstoss, B.A.; Weigel, P.H.
Site-directed mutation of conserved cysteine residues does not inactivate the Streptococcus pyogenes hyaluronan synthase
Glycobiology
11
1017-1024
2001
Streptococcus pyogenes
brenda
Asplund, T.; Brinck, J.; Suzuki, M.; Briskin, M.J.; Heldin, P.
Characterization of hyaluronan synthase from a human glioma cell line
Biochim. Biophys. Acta
1380
377-388
1998
Homo sapiens
brenda
Klewes, L.; Prehm, P.
Intracellular signal transduction for serum activation of the hyaluronan synthase in eukaryotic cell lines
J. Cell. Physiol.
160
539-544
1994
Mus musculus
brenda
Sayo, T.; Sugiyama, Y.; Takahashi, Y.; Ozawa, N.; Sakai, S.; Ishikawa, O.; Tamura, M.; Inoue, S.
Hyaluronan synthase 3 regulates hyaluronan synthesis in cultured human keratinocytes
J. Invest. Dermatol.
118
43-48
2002
Homo sapiens
brenda
Uchiyama, T.; Sakuta, T.; Kanayama, T.
Regulation of hyaluronan synthases in mouse uterine cervix
Biochem. Biophys. Res. Commun.
327
927-932
2005
Mus musculus
brenda
Tlapak-Simmons, V.L.; Baron, C.A.; Weigel, P.H.
Characterization of the purified hyaluronan synthase from Streptococcus equisimilis
Biochemistry
43
9234-9242
2004
Streptococcus dysgalactiae subsp. equisimilis
brenda
Jing, W.; DeAngelis, P.L.
Analysis of the two active sites of the hyaluronan synthase and the chondroitin synthase of Pasteurella multocida
Glycobiology
13
661-671
2003
Pasteurella multocida, Pasteurella multocida type A
brenda
Kumari, K.; Weigel, P.H.
Identification of a membrane-localized cysteine cluster near the substrate-binding sites of the Streptococcus equisimilis hyaluronan synthase
Glycobiology
15
529-539
2005
Streptococcus dysgalactiae subsp. equisimilis
brenda
Itano, N.; Kimata, K.
Mammalian hyaluronan synthases
IUBMB Life
54
195-199
2002
Homo sapiens, Mus musculus
brenda
Weigel, P.H.
Functional characteristics and catalytic mechanisms of the bacterial hyaluronan synthases
IUBMB Life
54
201-211
2002
Pasteurella multocida, Streptococcus pyogenes
brenda
Kumari, K.; Tlapak-Simmons, V.L.; Baggenstoss, B.A.; Weigel, P.H.
The streptococcal hyaluronan synthases are inhibited by sulfhydryl-modifying reagents, but conserved cysteine residues are not essential for enzyme function
J. Biol. Chem.
277
13943-13951
2002
Streptococcus dysgalactiae subsp. equisimilis, Streptococcus pyogenes (Q5X9A9), Streptococcus pyogenes
brenda
Pummill, P.E.; DeAngelis, P.L.
Evaluation of critical structural elements of UDP-sugar substrates and certain cysteine residues of a vertebrate hyaluronan synthase
J. Biol. Chem.
277
21610-21616
2002
Xenopus laevis
brenda
Itano, N.; Sawai, T.; Atsumi, F.; Miyaishi, O.; Taniguchi, S.; Kannagi, R.; Hamaguchi, M.; Kimata, K.
Selective expression and functional characteristics of three mammalian hyaluronan synthases in oncogenic malignant transformation
J. Biol. Chem.
279
18679-18687
2004
Rattus norvegicus (O35776), Rattus norvegicus (Q8CH92), Rattus norvegicus (Q8CH93)
brenda
Hoshi, H.; Nakagawa, H.; Nishiguchi, S.; Iwata, K.; Niikura, K.; Monde, K.; Nishimura, S.
An engineered hyaluronan synthase: characterization for recombinant human hyaluronan synthase 2 Escherichia coli
J. Biol. Chem.
279
2341-2349
2004
Homo sapiens
brenda
Tlapak-Simmons, V.L.; Baron, C.A.; Gotschall, R.; Haque, D.; Canfield, W.M.; Weigel, P.H.
Hyaluronan biosynthesis by class I streptococcal hyaluronan synthases occurs at the reducing end
J. Biol. Chem.
280
13012-13018
2005
Streptococcus dysgalactiae subsp. equisimilis, Streptococcus pyogenes
brenda
Rilla, K.; Siiskonen, H.; Spicer, A.P.; Hyttinen, J.M.; Tammi, M.I.; Tammi, R.H.
Plasma membrane residence of hyaluronan synthase is coupled to its enzymatic activity
J. Biol. Chem.
280
31890-31897
2005
Mus musculus
brenda
Krupa, J.C.; Shaya, D.; Chi, L.; Linhardt, R.J.; Cygler, M.; Withers, S.G.; Mort, J.S.
Quantitative continuous assay for hyaluronan synthase
Anal. Biochem.
361
218-225
2007
Pasteurella multocida
brenda
Goentzel, B.J.; Weigel, P.H.; Steinberg, R.A.
Recombinant human hyaluronan synthase 3 is phosphorylated in mammalian cells
Biochem. J.
396
347-354
2006
Homo sapiens (O00219), Homo sapiens
brenda
Pummill, P.E.; Kane, T.A.; Kempner, E.S.; DeAngelis, P.L.
The functional molecular mass of the Pasteurella hyaluronan synthase is a monomer
Biochim. Biophys. Acta
1770
286-290
2007
Pasteurella multocida
brenda
Adamia, S.; Reiman, T.; Crainie, M.; Mant, M.J.; Belch, A.R.; Pilarski, L.M.
Intronic splicing of hyaluronan synthase 1 (HAS1): a biologically relevant indicator of poor outcome in multiple myeloma
Blood
105
4836-4844
2005
Homo sapiens (Q92839), Homo sapiens
brenda
Tien, J.Y.; Spicer, A.P.
Three vertebrate hyaluronan synthases are expressed during mouse development in distinct spatial and temporal patterns
Dev. Dyn.
233
130-141
2005
Mus musculus (O08650), Mus musculus (P70312), Mus musculus (Q61647), Mus musculus
brenda
Jong, A.; Wu, C.H.; Chen, H.M.; Luo, F.; Kwon-Chung, K.J.; Chang, Y.C.; Lamunyon, C.W.; Plaas, A.; Huang, S.H.
Identification and characterization of CPS1 as a hyaluronic acid synthase contributing to the pathogenesis of C. neoformans infection
Eukaryot. Cell
6
1486-1496
2007
Cryptococcus neoformans
brenda
Nishida, Y.; Knudson, W.; Knudson, C.B.; Ishiguro, N.
Antisense inhibition of hyaluronan synthase-2 in human osteosarcoma cells inhibits hyaluronan retention and tumorigenicity
Exp. Cell Res.
307
194-203
2005
Homo sapiens (Q92819), Homo sapiens
brenda
Nikitovic, D.; Zafiropoulos, A.; Katonis, P.; Tsatsakis, A.; Theocharis, A.D.; Karamanos, N.K.; Tzanakakis, G.N.
Transforming growth factor-beta as a key molecule triggering the expression of versican isoforms v0 and v1, hyaluronan synthase-2 and synthesis of hyaluronan in malignant osteosarcoma cells
IUBMB Life
58
47-53
2006
Homo sapiens (Q92819), Homo sapiens
brenda
Kumari, K.; Baggenstoss, B.A.; Parker, A.L.; Weigel, P.H.
Mutation of two intramembrane polar residues conserved within the hyaluronan synthase family alters hyaluronan product size
J. Biol. Chem.
281
11755-11760
2006
Streptococcus dysgalactiae subsp. equisimilis
brenda
Weigel, P.H.; Kyossev, Z.; Torres, L.C.
Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase
J. Biol. Chem.
281
36542-36551
2006
Streptococcus dysgalactiae subsp. equisimilis
brenda
Tracy, B.S.; Avci, F.Y.; Linhardt, R.J.; DeAngelis, P.L.
Acceptor specificity of the Pasteurella hyaluronan and chondroitin synthases and production of chimeric glycosaminoglycans
J. Biol. Chem.
282
337-344
2007
Pasteurella multocida
brenda
Wilkinson, T.S.; Bressler, S.L.; Evanko, S.P.; Braun, K.R.; Wight, T.N.
Overexpression of hyaluronan synthases alters vascular smooth muscle cell phenotype and promotes monocyte adhesion
J. Cell. Physiol.
206
378-385
2006
Mus musculus
brenda
Adams, J.R.; Sander, G.; Byers, S.
Expression of hyaluronan synthases and hyaluronidases in the MG63 osteoblast cell line
Matrix Biol.
25
40-46
2006
Homo sapiens (O00219), Homo sapiens (Q92819)
brenda
Kyossev, Z.; Weigel, P.H.
An enzyme capture assay for analysis of active hyaluronan synthases
Anal. Biochem.
371
62-70
2007
Homo sapiens, Streptococcus dysgalactiae subsp. equisimilis
brenda
Kakizaki, I.; Itano, N.; Kimata, K.; Hanada, K.; Kon, A.; Yamaguchi, M.; Takahashi, T.; Takagaki, K.
Up-regulation of hyaluronan synthase genes in cultured human epidermal keratinocytes by UVB irradiation
Arch. Biochem. Biophys.
471
85-93
2008
Homo sapiens
brenda
Li, L.; Asteriou, T.; Bernert, B.; Heldin, C.H.; Heldin, P.
Growth factor regulation of hyaluronan synthesis and degradation in human dermal fibroblasts: importance of hyaluronan for the mitogenic response of PDGF-BB
Biochem. J.
404
327-336
2007
Homo sapiens, Mus musculus
brenda
Campo, G.M.; Avenoso, A.; Campo, S.; DAscola, A.; Ferlazzo, A.M.; Calatroni, A.
Differential effect of growth factors on hyaluronan synthase gene expression in fibroblasts exposed to oxidative stress
Biochemistry
72
974-982
2007
Homo sapiens
brenda
Stuhlmeier, K.M.
Prostaglandin E2: A potent activator of hyaluronan synthase 1 in type-B-synoviocytes
Biochim. Biophys. Acta
1770
121-129
2007
Homo sapiens
brenda
Allison, D.D.; Vasco, N.; Braun, K.R.; Wight, T.N.; Grande-Allen, K.J.
The effect of endogenous overexpression of hyaluronan synthases on material, morphological, and biochemical properties of uncrosslinked collagen biomaterials
Biomaterials
28
5509-5517
2007
Rattus norvegicus
brenda
Allison, D.D.; Wight, T.N.; Ripp, N.J.; Braun, K.R.; Grande-Allen, K.J.
Endogenous overexpression of hyaluronan synthases within dynamically cultured collagen gels: Implications for vascular and valvular disease
Biomaterials
29
2969-2976
2008
Rattus norvegicus
brenda
Mao, Z.; Chen, R.R.
Recombinant synthesis of hyaluronan by Agrobacterium sp
Biotechnol. Prog.
23
1038-1042
2007
Pasteurella multocida (Q7BLV3), Pasteurella multocida
brenda
Bartolo, R.C.; Donald, J.A.
The distribution of renal hyaluronan and the expression of hyaluronan synthases during water deprivation in the Spinifex hopping mouse, Notomys alexis
Comp. Biochem. Physiol. A
148
853-860
2007
Notomys alexis (Q27J86), Notomys alexis (Q27J87), Notomys alexis (Q27J88)
brenda
Nishitsuka, K.; Kashiwagi, Y.; Tojo, N.; Kanno, C.; Takahashi, Y.; Yamamoto, T.; Heldin, P.; Yamashita, H.
Hyaluronan production regulation from porcine hyalocyte cell line by cytokines
Exp. Eye Res.
85
539-545
2007
Sus scrofa
brenda
Bourguignon, L.Y.; Gilad, E.; Peyrollier, K.
Heregulin-mediated ErbB2-ERK signaling activates hyaluronan synthases leading to CD44-dependent ovarian tumor cell growth and migration
J. Biol. Chem.
282
19426-19441
2007
Homo sapiens (Q92819), Homo sapiens (Q92839), Homo sapiens (Q96RV2), Homo sapiens
brenda
Bharadwaj, A.G.; Rector, K.; Simpson, M.A.
Inducible hyaluronan production reveals differential effects on prostate tumor cell growth and tumor angiogenesis
J. Biol. Chem.
282
20561-20572
2007
Homo sapiens
brenda
Meran, S.; Thomas, D.; Stephens, P.; Martin, J.; Bowen, T.; Phillips, A.; Steadman, R.
Involvement of hyaluronan in regulation of fibroblast phenotype
J. Biol. Chem.
282
25687-25697
2007
Homo sapiens
brenda
Stuhlmeier, K.M.
Hyaluronan production in synoviocytes as a consequence of viral infections: HAS1 activation by Epstein-Barr virus and synthetic double- and single-stranded viral RNA analogs
J. Biol. Chem.
283
16781-16789
2008
Homo sapiens
brenda
Carulli, D.; Rhodes, K.E.; Fawcett, J.W.
Upregulation of aggrecan, link protein 1, and hyaluronan synthases during formation of perineuronal nets in the rat cerebellum
J. Comp. Neurol.
501
83-94
2007
Rattus norvegicus
brenda
Sim, G.S.; Lee, D.H.; Kim, J.H.; An, S.K.; Choe, T.B.; Kwon, T.J.; Pyo, H.B.; Lee, B.C.
Black rice (Oryza sativa L. var. japonica) hydrolyzed peptides induce expression of hyaluronan synthase 2 gene in HaCaT keratinocytes
J. Microbiol. Biotechnol.
17
271-279
2007
Homo sapiens (Q92819), Homo sapiens
brenda
Fischer, J.W.; Schroer, K.
Regulation of hyaluronan synthesis by vasodilatory prostaglandins. Implications for atherosclerosis
Thromb. Haemost.
98
287-295
2007
Mammalia
brenda
Sheng, J.Z.; Ling, P.X.; Zhu, X.Q.; Guo, X.P.; Zhang, T.M.; He, Y.L.; Wang, F.S.
Use of induction promoters to regulate hyaluronan synthase and UDP-glucose-6-dehydrogenase of Streptococcus zooepidemicus expression in Lactococcus lactis: a case study of the regulation mechanism of hyaluronic acid polymer
J. Appl. Microbiol.
107
136-144
2009
Streptococcus equi subsp. zooepidemicus
brenda
David-Raoudi, M.; Deschrevel, B.; Leclercq, S.; Galera, P.; Boumediene, K.; Pujol, J.P.
Chondroitin sulfate increases hyaluronan production by human synoviocytes through differential regulation of hyaluronan synthases: Role of p38 and Akt
Arthritis Rheum.
60
760-770
2009
Homo sapiens (O00219), Homo sapiens (Q92819), Homo sapiens (Q92839), Homo sapiens
brenda
Berdiaki, A.; Nikitovic, D.; Tsatsakis, A.; Katonis, P.; Karamanos, N.K.; Tzanakakis, G.N.
bFGF induces changes in hyaluronan synthase and hyaluronidase isoform expression and modulates the migration capacity of fibrosarcoma cells
Biochim. Biophys. Acta
1790
1258-1265
2009
Homo sapiens (Q92839)
brenda
Miyake, Y.; Sakurai, M.; Tanaka, S.; Tunjung, W.A.; Yokoo, M.; Matsumoto, H.; Aso, H.; Yamaguchi, T.; Sato, E.
Expression of hyaluronan synthase 1 and distribution of hyaluronan during follicular atresia in pig ovaries
Biol. Reprod.
80
249-257
2009
Sus scrofa
brenda
Adamia, S.; Reichert, A.A.; Kuppusamy, H.; Kriangkum, J.; Ghosh, A.; Hodges, J.J.; Pilarski, P.M.; Treon, S.P.; Mant, M.J.; Reiman, T.; Belch, A.R.; Pilarski, L.M.
Inherited and acquired variations in the hyaluronan synthase 1 (HAS1) gene may contribute to disease progression in multiple myeloma and Waldenstrom macroglobulinemia
Blood
112
5111-5121
2008
Homo sapiens (Q92839), Homo sapiens
brenda
Nykopp, T.; Rilla, K.; Sironen, R.; Tammi, M.; Tammi, R.; Hmlinen, K.; Heikkinen, A.; Komulainen, M.; Kosma, V.; Anttila, M.
Expression of hyaluronan synthases (HAS1-3) and hyaluronidases (HYAL1-2) in serous ovarian carcinomas: Inverse correlation between HYAL1 and hyaluronan content
BMC Cancer
9
143
2009
Homo sapiens (O00219), Homo sapiens (Q92819)
brenda
Campo, G.M.; Avenoso, A.; Campo, S.; DAscola, A.; Traina, P.; Calatroni, A.
Effect of cytokines on hyaluronan synthase activity and response to oxidative stress by fibroblasts
Br. J. Biomed. Sci.
66
28-36
2009
Homo sapiens (O00219), Homo sapiens (Q92819), Homo sapiens (Q92839)
brenda
Kultti, A.; Pasonen-Seppaenen, S.; Jauhiainen, M.; Rilla, K.J.; Kaernae, R.; Pyoeriae, E.; Tammi, R.H.; Tammi, M.I.
4-Methylumbelliferone inhibits hyaluronan synthesis by depletion of cellular UDP-glucuronic acid and downregulation of hyaluronan synthase 2 and 3
Exp. Cell Res.
315
1914-1923
2009
Homo sapiens (O00219), Homo sapiens (Q92819)
brenda
Makkonen, K.M.; Pasonen-Seppaenen, S.; Toerroenen, K.; Tammi, M.I.; Carlberg, C.
Regulation of the hyaluronan synthase 2 gene by convergence in cyclic AMP response element-binding protein and retinoid acid receptor signaling
J. Biol. Chem.
284
18270-18281
2009
Homo sapiens (Q92819), Homo sapiens
brenda
Ghosh, A.; Kuppusamy, H.; Pilarski, L.M.
Aberrant splice variants of HAS1 (hyaluronan synthase 1) multimerize with and modulate normally spliced HAS1 protein: a potential mechanism promoting human cancer
J. Biol. Chem.
284
18840-18850
2009
Homo sapiens (Q92839), Homo sapiens
brenda
Vigetti, D.; Genasetti, A.; Karousou, E.; Viola, M.; Clerici, M.; Bartolini, B.; Moretto, P.; De Luca, G.; Hascall, V.C.; Passi, A.
Modulation of hyaluronan synthase activity in cellular membrane fractions
J. Biol. Chem.
284
30684-30694
2009
Homo sapiens
brenda
Ruegheimer, L.; Olerud, J.; Johnsson, C.; Takahashi, T.; Shimizu, K.; Hansell, P.
Hyaluronan synthases and hyaluronidases in the kidney during changes in hydration status
Matrix Biol.
28
390-395
2009
Rattus norvegicus, Rattus norvegicus (O35776)
brenda
Dunn, K.M.; Lee, P.K.; Wilson, C.M.; Iida, J.; Wasiluk, K.R.; Hugger, M.; McCarthy, J.B.
Inhibition of hyaluronan synthases decreases matrix metalloproteinase-7 (MMP-7) expression and activity
Surgery
145
322-329
2009
Homo sapiens (O00219), Homo sapiens (Q92819)
brenda
Medina, A.P.; Lin, J.; Weigel, P.H.
Hyaluronan synthase mediates dye translocation across liposomal membranes
BMC Biochem.
13
2-2
2012
Streptococcus dysgalactiae subsp. equisimilis
brenda
Nykopp, T.K.; Rilla, K.; Tammi, M.I.; Tammi, R.H.; Sironen, R.; Haemaelaeinen, K.; Kosma, V.M.; Heinonen, S.; Anttila, M.
Hyaluronan synthases (HAS1-3) and hyaluronidases (HYAL1-2) in the accumulation of hyaluronan in endometrioid endometrial carcinoma
BMC Cancer
10
512
2010
Homo sapiens
brenda
Caskey, R.C.; Allukian, M.; Lind, R.C.; Herdrich, B.J.; Xu, J.; Radu, A.; Mitchell, M.E.; Liechty, K.W.
Lentiviral-mediated over-expression of hyaluronan synthase-1 (HAS-1) decreases the cellular inflammatory response and results in regenerative wound repair
Cell Tissue Res.
351
117-125
2013
Mus musculus, Mus musculus C57BL/6
brenda
Weigel, P.H.; Baggenstoss, B.A.
Hyaluronan synthase polymerizing activity and control of product size are discrete enzyme functions that can be uncoupled by mutagenesis of conserved cysteines
Glycobiology
22
1302-1310
2012
Streptococcus dysgalactiae subsp. equisimilis
brenda
Karousou, E.; Kamiryo, M.; Skandalis, S.S.; Ruusala, A.; Asteriou, T.; Passi, A.; Yamashita, H.; Hellman, U.; Heldin, C.H.; Heldin, P.
The activity of hyaluronan synthase 2 is regulated by dimerization and ubiquitination
J. Biol. Chem.
285
23647-23654
2010
Mus musculus
brenda
Vigetti, D.; Clerici, M.; Deleonibus, S.; Karousou, E.; Viola, M.; Moretto, P.; Heldin, P.; Hascall, V.C.; De Luca, G.; Passi, A.
Hyaluronan synthesis is inhibited by adenosine monophosphate-activated protein kinase through the regulation of HAS2 activity in human aortic smooth muscle cells
J. Biol. Chem.
286
7917-7924
2011
Homo sapiens (Q92819)
brenda
Vigetti, D.; Deleonibus, S.; Moretto, P.; Karousou, E.; Viola, M.; Bartolini, B.; Hascall, V.C.; Tammi, M.; De Luca, G.; Passi, A.
Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis
J. Biol. Chem.
287
35544-35555
2012
Homo sapiens
brenda
Rilla, K.; Oikari, S.; Jokela, T.A.; Hyttinen, J.M.; Kaernae, R.; Tammi, R.H.; Tammi, M.I.
Hyaluronan synthase 1 (HAS1) requires higher cellular UDP-GlcNAc concentration than HAS2 and HAS3
J. Biol. Chem.
288
5973-5983
2013
Homo sapiens (O00219), Homo sapiens (Q92819), Homo sapiens (Q92839), Homo sapiens
brenda
Hubbard, C.; McNamara, J.T.; Azumaya, C.; Patel, M.S.; Zimmer, J.
The hyaluronan synthase catalyzes the synthesis and membrane translocation of hyaluronan
J. Mol. Biol.
418
21-31
2012
Streptococcus dysgalactiae subsp. equisimilis
brenda
Pure, E.; Krolikoski, M.; Monslow, J.
Role for hyaluronan synthase 3 in the response to vascular injury
Arterioscler. Thromb. Vasc. Biol.
36
224-225
2016
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
brenda
Siiskonen, H.; Kaernae, R.; Hyttinen, J.M.; Tammi, R.H.; Tammi, M.I.; Rilla, K.
Hyaluronan synthase 1 (HAS1) produces a cytokine-and glucose-inducible, CD44-dependent cell surface coat
Exp. Cell Res.
320
153-163
2014
Homo sapiens
brenda
Takabe, P.; Bart, G.; Ropponen, A.; Rilla, K.; Tammi, M.; Tammi, R.; Pasonen-Seppaenen, S.
Hyaluronan synthase 3 (HAS3) overexpression downregulates MV3 melanoma cell proliferation, migration and adhesion
Exp. Cell Res.
337
1-15
2015
Homo sapiens
brenda
Siiskonen, H.; Oikari, S.; Pasonen-Seppaenen, S.; Rilla, K.
Hyaluronan synthase 1: a mysterious enzyme with unexpected functions
Front. Immunol.
6
43
2015
Homo sapiens (Q92839)
brenda
Toerroenen, K.; Nikunen, K.; Kaernae, R.; Tammi, M.; Tammi, R.; Rilla, K.
Tissue distribution and subcellular localization of hyaluronan synthase isoenzymes
Histochem. Cell Biol.
141
17-31
2014
Mus musculus (O08650), Mus musculus (P70312), Mus musculus (Q61647), Mus musculus
brenda
Kooy, F.; Beeftink, H.; Eppink, M.; Tramper, J.; Eggink, G.; Boeriu, C.
Kinetic and structural analysis of two transferase domains in Pasteurella multocida hyaluronan synthase
J. Mol. Catal. B
102
138-145
2014
Pasteurella multocida (Q7BLV3)
-
brenda
Vigetti, D.; Viola, M.; Karousou, E.; De Luca, G.; Passi, A.
Metabolic control of hyaluronan synthases
Matrix Biol.
35
8-13
2014
Mammalia, Streptococcus sp., Pasteurella multocida (Q7BLV3)
brenda
Li, Y.; Liang, J.; Yang, T.; Monterrosa Mena, J.; Huan, C.; Xie, T.; Kurkciyan, A.; Liu, N.; Jiang, D.; Noble, P.W.
Hyaluronan synthase 2 regulates fibroblast senescence in pulmonary fibrosis
Matrix Biol.
55
35-48
2016
Mus musculus (P70312), Mus musculus
brenda
Garoby-Salom, S.; Rouahi, M.; Mucher, E.; Auge, N.; Salvayre, R.; Negre-Salvayre, A.
Hyaluronan synthase-2 upregulation protects smpd3-deficient fibroblasts against cell death induced by nutrient deprivation, but not against apoptosis evoked by oxidized LDL
Redox Biol.
4
118-126
2015
Mus musculus (P70312), Mus musculus 129/Sv (P70312)
brenda
Chavoshinejad, R.; Marei, W.F.; Hartshorne, G.M.; Fouladi-Nashta, A.A.
Localisation and endocrine control of hyaluronan synthase (HAS) 2, HAS3 and CD44 expression in sheep granulosa cells
Reprod. Fertil. Dev.
28
765-775
2016
Ovis aries, Ovis aries (W5PN25), Ovis aries (W5PZY5)
brenda
Eisele, A.; Zaun, H.; Kuballa, J.; Elling, L.
In vitro one-pot enzymatic synthesis of hyaluronic acid from sucrose and N-acetylglucosamine optimization of the enzyme module system and nucleotide sugar regeneration
ChemCatChem
10
2969-2981
2018
Pasteurella multocida (Q7BLV3)
-
brenda
Yang, J.; Cheng, F.; Yu, H.; Wang, J.; Guo, Z.; Stephanopoulos, G.
Key role of the carboxyl terminus of hyaluronan synthase in processive synthesis and size control of hyaluronic acid polymers
Biomacromolecules
18
1064-1073
2017
Streptococcus dysgalactiae subsp. equisimilis (A0A514TRT9), Streptococcus dysgalactiae subsp. equisimilis
brenda
Zhang, L.; Huang, H.; Wang, H.; Chen, J.; Du, G.; Kang, Z.
Rapid evolution of hyaluronan synthase to improve hyaluronan production and molecular mass in Bacillus subtilis
Biotechnol. Lett.
38
2103-2108
2016
Streptococcus equi subsp. zooepidemicus (Q84GC8), Streptococcus equi subsp. zooepidemicus
brenda
Passi, A.; Vigetti, D.; Buraschi, S.; Iozzo, R.V.
Dissecting the role of hyaluronan synthases in the tumor microenvironment
FEBS J.
286
2937-2949
2019
Mus musculus (P70312), Homo sapiens (Q92819)
brenda
Weigel, P.H.; Baggenstoss, B.A.; Washburn, J.L.
Hyaluronan synthase assembles hyaluronan on a [GlcNAc(beta1,4)]n-GlcNAc(alpha1->)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end
Glycobiology
27
536-554
2017
Streptococcus dysgalactiae subsp. equisimilis (A0A514TRT9), Streptococcus dysgalactiae subsp. equisimilis
brenda
Yoshida, H.; Aoki, M.; Komiya, A.; Endo, Y.; Kawabata, K.; Nakamura, T.; Sakai, S.; Sayo, T.; Okada, Y.; Takahashi, Y.
HYBID (alias KIAA1199/CEMIP) and hyaluronan synthase coordinately regulate hyaluronan metabolism in histamine-stimulated skin fibroblasts
J. Biol. Chem.
295
2483-2494
2020
Homo sapiens (Q92819), Homo sapiens
brenda
Yang, G.; Jiang, B.; Cai, W.; Liu, S.; Zhao, S.
Hyaluronan and hyaluronan synthases expression and localization in embryonic mouse molars
J. Mol. Histol.
47
413-420
2016
Mus musculus (O08650), Mus musculus (P70312), Mus musculus (Q61647)
brenda
Lai, Z.; Teo, C.
Cloning and expression of hyaluronan synthase (hasA) in recombinant Escherichia coli BL21 and its hyaluronic acid production in shake flask culture
Malays. J. Microbiol.
15
575-582
2019
Streptococcus equi subsp. zooepidemicus (Q84GC8)
-
brenda
Homann, S.; Grandoch, M.; Kiene, L.S.; Podsvyadek, Y.; Feldmann, K.; Rabausch, B.; Nagy, N.; Lehr, S.; Kretschmer, I.; Oberhuber, A.; Bollyky, P.; Fischer, J.W.
Hyaluronan synthase 3 promotes plaque inflammation and atheroprogression
Matrix Biol.
66
67-80
2018
Mus musculus (O08650)
brenda
Mehic, M.; de Sa, V.K.; Hebestreit, S.; Heldin, C.H.; Heldin, P.
The deubiquitinating enzymes USP4 and USP17 target hyaluronan synthase 2 and differentially affect its function
Oncogenesis
6
e348
2017
Homo sapiens (Q92819), Homo sapiens
brenda
Agarwal, G.; K V, K.; Prasad, S.B.; Bhaduri, A.; Jayaraman, G.
Biosynthesis of Hyaluronic acid polymer Dissecting the role of sub structural elements of hyaluronan synthase
Sci. Rep.
9
12510
2019
Streptococcus equi subsp. zooepidemicus (Q84GC8)
brenda
Yang, Y.M.; Noureddin, M.; Liu, C.; Ohashi, K.; Kim, S.Y.; Ramnath, D.; Powell, E.E.; Sweet, M.J.; Roh, Y.S.; Hsin, I.F.; Deng, N.; Liu, Z.; Liang, J.; Mena, E.; Shouhed, D.; Schwabe, R.F.; Jiang, D.; Lu, S.C.; Noble, P.W.; Seki, E.
Hyaluronan synthase 2-mediated hyaluronan production mediates Notch1 activation and liver fibrosis
Sci. Transl. Med.
11
eaat9284
2019
Mus musculus (P70312), Mus musculus, Homo sapiens (Q92819), Homo sapiens
brenda