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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
active site structure
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
5-step reaction mechanism, catalytic residues are Arg349, His399, Tyr40, residues responsible for substrate binding and translocation of the remaining substrate are Arg243and Asn580, enzyme and acitive site strucure
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
active site structure and substrate binding of wild-type and mutant enzymes with chondroitin, mode of action
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
Streptomyces hyalurolytics
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
Streptomyces hyalurolyticus
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose, catalytic mechanism
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose, substrate binding site
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
also acts on chondroitin, the product is more systematically known as 3-(4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-glucose, substrate binding site
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
Asn349, His399, and Tyr408 are involved in catalysis, flexible, allosteric behavior of the enzyme, mechanism, active site structure and substrate binding and interactions, overview
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
catalytic mechanism, substrate binding, structure modeling, residues Tyr408, Asn349, and His399 are involved in catalysis and important
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
catalytic mechanism, the flexibility of the enzyme structure is important, the beta-domain is involved in the progressive catalytic process, enzyme substrate interactions
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
enzyme-product interaction from crystal structure, catalytic mechanism, interaction with substrate binding site, Tyr408, Asn349, and His399 are involved
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
His479 is critical for activity, active site structure, mechanism
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
lyase mechanism, elimination process
Streptomyces hyalurolyticus
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
processive reaction mode, catalytic mechanism, catalytic residues are Asn349, His399, and Tyr408, residues responsible for product release are Glu388, Asp398, and Thr400, the socalled negative patch, residues responsible for correct substrate positioning are Trp291, Trp292, and Phe343, the socalled hydrophobic patch, substrate binding structure of wild-type and mutant enzymes
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
rapid elimination mechanism
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
substrate binding, structure and mechanims, and reaction mechanism, catalytic residues are His479, Tyr488, and Asn429, modeling of binding of a tetrasaccharide in the active site cleft
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
active site structure and hydrophobic patch, molecular mechanism, enzyme flexibility and structural requirements
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
active site structure and hydrophobic patch, molecular mechanism, enzyme flexibility and structural requirements
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
binding of negatively charged hydrophobic substrates is facilitated by the predominantly positive and hydrophobic cleft located at distorted (alpha/alpha)5-6 barrel, mechanism of hyaluronan degradation, active site residues are Asn349, His399, and Tyr408, overview
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
binding of negatively charged hydrophobic substrates is facilitated by the predominantly positive and hydrophobic cleft located at distorted (alpha/alpha)5-6 barrel, mechanism of hyaluronan degradation, overview
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
catalytic reaction mechanism and structural requirements, catalytic residues are Asn349, His399, and Tyr408
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
catalytic reaction mechanism and structural requirements, catalytic residues are Asn429, His479, and Tyr488, a required hydrophobic patch is composed of residues Glu468, Asp478, and Thr480
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[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
catalytic residues are Asn349, His399, and Tyr408
Q6H8W8, Q6H8W9, Q6H8X0, Q6H8X1, Q6H8X2, Q6H8X4, Q6H8X5, Q6H8X6, Q6H8X7, Q6H8X8, Q6H8Y0, Q6H8Y1, Q6H8Y2, Q6H8Y3, Q6H8Y4, Q8VLQ7, Q8VLQ8
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
catalytic residues are Asn349, His399, and Tyr408
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
mechanism of hyaluronan degradation, random endolytic action pattern, overview
Streptomyces hyalurolyticus
-
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
along with the substrate binding, the phenylhydroxyl hydrogen atom of Tyr408 will transfer to nearby His399 via a near barrierless transition state, which results in a negatively charged Tyr408 and positively charged His399. The Tyr408, rather than the previously proposed His399, acts as the general base for the subsequent beta-elimination reaction. The His399 has the function of neutralizing the C5-carboxyl group, reaction mechanism, overview
-
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate
binding of the substrate molecule can lead to the ionization of Y408 and protonation of H399, Y408 serves as the general base in the proton abstraction, while general acid is the next proton donation step. The reaction can be classified into syn elimination reaction mechanism, reaction mechanism analysis, detailed overview
-
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chondroitin
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-galactosamine + ?
non-progressive mode
unsaturated disaccharide units
-
?
chondroitin 4-sulfate
?
-
weak activity
-
-
?
chondroitin 6-sulfate
?
-
weak activity
-
-
?
chondroitin sulfate
GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate + GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)
-
-
-
-
?
chondroitin sulfate C
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-galactose
hyaluronan
2-acetamido-2-deoxy-3-(beta-D-4-deoxy-gluco-4-enepyranosyluronic acid)-glucose + ?
-
-
-
-
?
hyaluronan
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-glucose
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
hyaluronan
fully O-sulfated oligosaccharides
Streptomyces hyalurolyticus
-
from Streptococcus zooepidemicus, sodium salt, large scale depolymerization
chain length of 4-20, detection and composition analysis
-
?
hyaluronan
hyaluronic acid oligomers
hyaluronan + 2 H2O
N-acetyl-beta-D-glucosamine + D-glucuronate + ?
Streptomyces hyalurolyticus
-
from Streptococcus zooepidemicus, degradation
-
-
?
hyaluronan + H2O
oligosaccharides
-
specific for, degradation
-
-
?
hyaluronan hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
hyaluronan tetrasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
unsaturated disaccharide units
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
hyaluronate
?
-
efficient degradation of hyaluronate
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
hyaluronate hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
unsaturated disaccharide
-
?
hyaluronic acid
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
hyaluronic acid
hyaluronic acid oligomers
hyaluronic acid
hyaluronic acid oligosaccharides
-
-
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
hyaluronic acid polymer
hyaluronic acid tetrasaccharide + hyaluronic acid hexasaccharide
Streptomyces hyalurolyticus
-
hyaluronic acid purified from Mytilus galloprovincialis
-
-
?
tetrasaccharides with a 6-sulfated disaccharide at the reducing end
?
-
-
-
-
?
additional information
?
-
chondroitin sulfate
?
-
-
-
-
ir
chondroitin sulfate
?
degradation
-
-
?
chondroitin sulfate
?
degrades progressively unsulfated and 6-sulfated regions from the reducing end
-
-
?
chondroitin sulfate
?
degradation
-
-
?
chondroitin sulfate
?
non-progressive mode, no activity with chondroitin 4-sulfated at the nonreducing end, no activity with substrate sulfated at position 2
-
-
?
chondroitin sulfate
?
-
-
-
-
?
chondroitin sulfate A
?
-
24.7% of the activity with hyaluronate
-
-
?
chondroitin sulfate A
?
-
24.7% of the activity with hyaluronate
-
-
?
chondroitin sulfate A
?
44% of the activity with hyaluronan
-
-
?
chondroitin sulfate A
?
44% of the activity with hyaluronan
-
-
?
chondroitin sulfate C
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-galactose
30% of the activity with hyaluronan
-
-
?
chondroitin sulfate C
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-galactose
30% of the activity with hyaluronan
-
-
?
hyaluronan
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-glucose
enzyme displays endo-type degratation. The viscosity of hyaluronan decreases to 37% of the original one after 3-min incubation
-
-
?
hyaluronan
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-glucose
enzyme displays endo-type degratation. The viscosity of hyaluronan decreases to 37% of the original one after 3-min incubation
-
-
?
hyaluronan
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-glucose
-
from human umbilical cord
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
from umbilical cord
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
enzyme might be involved in the pathogenicity of the bacterium causing paracocidiodomycosis
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
unsaturated disaccharide
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
disaccharide unit
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
elimination of the polymer in the host connective tissue
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
progressive degradation from the reducing end
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
substrate structure
disaccharide unit
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
unsaturated disaccharide units
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
disaccharide unit
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
degradation leads to increased permeability of the host tissue and therefore helps bacterial invasion
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
from human umbilical cord, degradation, from the reducing to the nonreducing end
unsaturated disaccharide units, product identification
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
progressive mode of action, degradation
unsaturated disaccharide unit
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
progressive mode, preferred substrate
unsaturated disaccharide units
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
substrate structure
disaccharide unit
-
ir
hyaluronan
?
-
-
-
?
hyaluronan
?
enzyme facilitates the invasion and spreading of the pathogenic bacterium in the host tissue by degrading the hosts' extracellular matrix component in connective tissue
-
-
?
hyaluronan
?
-
extracellular enzyme facilitates the invasion and spreading of the pathogenic bacterium in the host tissue by degrading the hosts' extracellular matrix component in connective tissue
-
-
?
hyaluronan
?
native enzyme and isolated N-terminal domain
-
-
?
hyaluronan
?
-
extracellular enzyme facilitates the invasion and spreading of the pathogenic bacterium in the host tissue by degrading the hosts' extracellular matrix component in connective tissue
-
-
?
hyaluronan
hyaluronic acid oligomers
degradation
-
-
?
hyaluronan
hyaluronic acid oligomers
degradation
-
-
?
hyaluronan
hyaluronic acid oligomers
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronan
hyaluronic acid oligomers
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronan hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
progressive mode of action, degradation
unsaturated disaccharide unit
-
?
hyaluronan hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
the longest segment that binds entirely within the active site, a cleft between alpha- and beta-domain
unsaturated disaccharide units
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
Streptomyces hyalurolyticus
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
eliminative reaction, degradation
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
3(DELTA-4,5-beta-D-glucuronosyl)-2-acetamido-2-deoxy-D-glucose
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
unsaturated disaccharide
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
-
unsaturated disaccharides are released from the end of the hyaluronan chains
?
hyaluronic acid
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
-
-
?
hyaluronic acid
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
Streptomyces hyalurolytics
-
from pig skin
-
-
?
hyaluronic acid
?
-
-
-
-
?
hyaluronic acid
?
-
from rooster comb
-
-
?
hyaluronic acid
?
-
-
-
-
?
hyaluronic acid
?
-
from rooster comb
-
-
?
hyaluronic acid
?
-
from pig skin
-
-
?
hyaluronic acid
?
no activity against chondroitin 4-sulfate, chondroitin 6-sulfate and dermatan sulfate
end-products are 4,5-unsaturated hyalurono-hexasaccharide and 4,5-unsaturated hyalurono-octasaccharide, with small amounts of 4,5-unsaturated hyalurono-tetrasaccharide, 4,5-unsaturated hyalurono-decasaccharide and longer oligosaccharides, early time points shows that a wide range of 4,5-unsaturated oligosaccharides are produced, indicating an endo-acting mode of digestion
-
?
hyaluronic acid
?
-
nonhydrolytic cleavage of the glycosidic bond, initiation of degradation activity analysis by molecular mechanical molecular dynamic simulations and free energy profiles, simulation and analysis of the enzyme-substrate complex structure, overview
-
-
?
hyaluronic acid
?
-
-
-
-
?
hyaluronic acid
?
the enzyme is a hyaluronic acid specific hyaluronate lyase showing ability to degrade hyaluronate to unsaturated disaccharide units
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion by subcutaneous infection, the enzyme is an essential bacterial virulence factor
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion by subcutaneous infection, the enzyme is an essential bacterial virulence factor
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
-
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
-
-
?
hyaluronic acid
hyaluronic acid oligomers
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
the enzyme is essential for growth on hyaluronate as carbon source
-
-
?
hyaluronic acid
hyaluronic acid oligomers
native and recombinant serotype 7 enzyme, human umbelical cord hyaluronate
-
-
?
hyaluronic acid
hyaluronic acid oligomers
Streptomyces hyalurolyticus
-
highly specific for hyaluronan, degradation, unsaturated products of varied size
-
-
?
hyaluronic acid
hyaluronic acid oligomers
Streptomyces hyalurolyticus
-
highly specific for hyaluronan
primarily disaccharides, but also tetrasaccharides and hexasaccharides
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
-
degradation
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
-
depolymerization
product identification by CE-MS, gel filtration, and viscosimetry
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
-
degradation
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
-
depolymerization
product identification by CE-MS, gel filtration, and viscosimetry
-
?
unsulfated chondroitin
?
degradation
-
-
?
unsulfated chondroitin
?
degradation
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
very poor substrate: chitosan. No substrates: heparin sodium, sodium alginate, carrageenan, pectin, soluble starch, xanthan gum
-
-
?
additional information
?
-
-
very poor substrate: chitosan. No substrates: heparin sodium, sodium alginate, carrageenan, pectin, soluble starch, xanthan gum
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis, enzyme may play a role in releasing nutrients thereby promoting establishment of the organism in the gut
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is the non-lethal Mu toxin, causes gas gangrene, produces many extracellular proteins during infection that are potetial virulence factors
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
chondroitin, 2.3% of the activity with hyaluronan
-
-
?
additional information
?
-
-
chondroitin, 2.3% of the activity with hyaluronan
-
-
?
additional information
?
-
chondroitin, 2.3% of the activity with hyaluronan
-
-
?
additional information
?
-
-
the minimum recognition and digestion domain is hyaluronic acid heptasaccharide. The enzyme cleaves both beta-1,4- and beta-1,3-glycosidic linkages. The resulting oligosaccharides, generated with a 2-acetamido-2,3-di-deoxy-beta-D-erythro-hex-2-enopyranose at the non-reducing end, are believed to be unstable and undergo breakdown immediately after their generation, and oligosaccharides with a 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid residue at the non-reducing end are formed
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
-
global regulators sar and agr are involved in enzyme regulation
-
-
?
additional information
?
-
-
global regulators sar and agr are involved in enzyme regulation
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
enzyme is a virulence factor that helps the pathogen to brake through the biophysical barrier of the host tissues
-
-
?
additional information
?
-
-
enzyme is a virulence factor that helps the pathogen to brake through the biophysical barrier of the host tissues
-
-
?
additional information
?
-
-
the enzyme contributes to the invasive capacity of the pathogenic organism by degrading hyaluronan and chondroitin sulfates of the extracellular matrix of host tissues
-
-
?
additional information
?
-
-
fragments from trypsin digestion are still active, enzyme is active in SDS-PAGE
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview
-
-
?
additional information
?
-
-
the enzyme also catalyzes the degradation of other polymeric glycans
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis, enzyme causes mastitis, may have an important role in promoting dissemination of the producing organism into host tissue
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis, strong association between the production of purulent abscesses and enzyme during infections
-
-
?
additional information
?
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
phylogenetic analysis, causes a number of different infections, including meningitis and pneumoniae, where the enzyme may function as a spreading factor, while pneumolysin acts as a toxin
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview
-
-
?
additional information
?
-
the enzyme also catalyzes the degradation of other polymeric glycans
-
-
?
additional information
?
-
-
C-terminal domain does not bind directly to the substrate, instead the domain contributes to the interaction with the polymeric hyaluronan for catalysis. Furthermore, the substrate specificity exchanges with the size of catalytic cleft. The role of linker connecting alpha-domain to C-terminal domain is found to hold the C-terminal domain in a conformation suitable for achieving maximum activity
-
-
?
additional information
?
-
-
mathematical model for the degradation of hyaluronan. The model is based on a processive kinetic mechanism and consists of a coupled system of nonlinear ordinary differential equations for the species of interest. The rate at which degradation proceeds is strongly dependent on the initial concentration of enzyme
-
-
?
additional information
?
-
-
phylogenetic analysis, anti-phagocytic factors, such as M-protein, might provide sufficient protection for Streptococcus pyogenes infection during enzyme production
-
-
?
additional information
?
-
-
substrate specificity, no activity with chonroitin, dermatan sulfate, keratan sulfate, heparin, chondroitin 4-sulfate and chondroitin 6-sulfate
-
-
?
additional information
?
-
-
substrate specificity, product indentification
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is involved in development of meningitis in infected pigs
-
-
?
additional information
?
-
-
the enzyme is involved in development of meningitis in infected pigs
-
-
?
additional information
?
-
-
phylogenetic analysis, enzyme causes mastitis, may have an important role in promoting dissemination of the producing organism into host tissue, anti-phagocytic factors in the capsule, such as M-protein, might provide sufficient protection for Streptococcus pyogenes infection during enzyme production
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
Streptomyces hyalurolyticus
-
hyaluronan is degraded by L-ascorbic acid, D-isoascorbic acid, and dehydroascorbic acid themselves, only slightly by L-gulonic-gamma-lactone, D-saccharic-1,4-lactone, and alpha-D-glucoheptonic-gamma-lactone
-
-
?
additional information
?
-
Streptomyces hyalurolyticus
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
hyaluronan
hyaluronic acid oligomers
hyaluronate
?
-
efficient degradation of hyaluronate
-
-
?
hyaluronic acid
hyaluronic acid oligomers
hyaluronic acid polymer
hyaluronic acid oligomers
additional information
?
-
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
enzyme might be involved in the pathogenicity of the bacterium causing paracocidiodomycosis
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
disaccharide unit
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
elimination of the polymer in the host connective tissue
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
-
disaccharide unit
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
degradation leads to increased permeability of the host tissue and therefore helps bacterial invasion
-
-
?
hyaluronan
?
-
-
-
?
hyaluronan
?
enzyme facilitates the invasion and spreading of the pathogenic bacterium in the host tissue by degrading the hosts' extracellular matrix component in connective tissue
-
-
?
hyaluronan
?
-
extracellular enzyme facilitates the invasion and spreading of the pathogenic bacterium in the host tissue by degrading the hosts' extracellular matrix component in connective tissue
-
-
?
hyaluronan
?
-
extracellular enzyme facilitates the invasion and spreading of the pathogenic bacterium in the host tissue by degrading the hosts' extracellular matrix component in connective tissue
-
-
?
hyaluronan
hyaluronic acid oligomers
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronan
hyaluronic acid oligomers
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronic acid
?
-
-
-
-
?
hyaluronic acid
?
-
-
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion by subcutaneous infection, the enzyme is an essential bacterial virulence factor
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion by subcutaneous infection, the enzyme is an essential bacterial virulence factor
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
the enzyme is essential for growth on hyaluronate as carbon source
-
-
?
hyaluronic acid
hyaluronic acid oligomers
Streptomyces hyalurolyticus
-
highly specific for hyaluronan, degradation, unsaturated products of varied size
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
-
degradation
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
-
degradation
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis, enzyme may play a role in releasing nutrients thereby promoting establishment of the organism in the gut
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis, enzyme is the non-lethal Mu toxin, causes gas gangrene, produces many extracellular proteins during infection that are potetial virulence factors
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
-
global regulators sar and agr are involved in enzyme regulation
-
-
?
additional information
?
-
-
global regulators sar and agr are involved in enzyme regulation
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
enzyme is a virulence factor that helps the pathogen to brake through the biophysical barrier of the host tissues
-
-
?
additional information
?
-
-
enzyme is a virulence factor that helps the pathogen to brake through the biophysical barrier of the host tissues
-
-
?
additional information
?
-
-
the enzyme contributes to the invasive capacity of the pathogenic organism by degrading hyaluronan and chondroitin sulfates of the extracellular matrix of host tissues
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis, enzyme causes mastitis, may have an important role in promoting dissemination of the producing organism into host tissue
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis, strong association between the production of purulent abscesses and enzyme during infections
-
-
?
additional information
?
-
phylogenetic analysis, causes a number of different infections, including meningitis and pneumoniae, where the enzyme may function as a spreading factor, while pneumolysin acts as a toxin
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview
-
-
?
additional information
?
-
-
phylogenetic analysis, anti-phagocytic factors, such as M-protein, might provide sufficient protection for Streptococcus pyogenes infection during enzyme production
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
-
the enzyme is a virulence factor of the animal pathogen, relation between enzyme activity, serotype, and disease state, overview
-
-
?
additional information
?
-
the enzyme is involved in development of meningitis in infected pigs
-
-
?
additional information
?
-
-
the enzyme is involved in development of meningitis in infected pigs
-
-
?
additional information
?
-
-
phylogenetic analysis, enzyme causes mastitis, may have an important role in promoting dissemination of the producing organism into host tissue, anti-phagocytic factors in the capsule, such as M-protein, might provide sufficient protection for Streptococcus pyogenes infection during enzyme production
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
additional information
?
-
Streptomyces hyalurolyticus
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
additional information
?
-
-
phylogenetic analysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(13Z)-docos-13-enoic acid
(25S)-(+)-12alpha-hydroxy-3alpha-methylcarboxyacetate-24-methyllanosta-8,24(31)-diene-26-oic acid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0035 mM
(2E)-1-furan-2-yl-3-(4-nitrophenyl)prop-2-en-1-one
IC50 at enzyme optimum pH 5.0 is 0.31 mM, and 0.16 mM at physiological pH 7.4
(3-chlorophenyl)(2-thioxo-1H-benzo[d]imidazol-1-yl)methanone
-
-
(E)-3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)prop-2-en-1-one
-
36% inhibition
1,10-phenanthroline
-
5 mM, 75% residual activity
1,3-benzoxazole-2(3H)-thione
-
-
1,3-diacetyl-1H-benzo[d]imidazol-2(3H)-one
-
10% inhibition
1,3-diacetyl-benzimidazole-2-thione
IC50 at enzyme optimum pH 5.0 is 0.16 mM, and 0.005 mM at physiological pH 7.4
1,3-diacetylbenzimidazole-2-thione
-
-
1,3-dihydro-2H-benzimidazole-2-thione
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)-3-phenylpropan-1-one
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)butan-1-one
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)ethanone
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)hexan-1-one
-
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)propan-1one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)decan-1-one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexadecan-1-one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexan-1-one
-
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
-
1-(3-acetyl-1,2-dihydro-2-thioxobenzo[d]imidazol-1-yl)hexan-1-one
-
-
1-(3-ethyl-1,2-dihydro-2-thioxobenzo[d]imidazole-1-yl)ethanone
-
-
1-decyl-2-(4-sulfamoyloxyphenyl)-1-indol-6-yl sulfamate
-
-
1-decyl-2-(4-sulfamoyloxyphenyl)-1H-indol-6-yl sulfamate
-
inhibitor fits in the enzymatic active site via interactions resembling the binding mode of the natural hyaluronan substrate
1-ethyl-1H-benzo[d]imidazole-2(3H)-thione
-
28% inhibition
2,2'-benzene-1,4-diyldiacetic acid
IC50 at enzyme optimum pH 5.0 is 0.37 mM, and 0.90 mM at physiological pH 7.4
2,3-Butanedione
-
inactivation, arginine-specific reagent
2-Hydroxy-5-nitrobenzylbromide
2.5 mM, 87.4% inhibition
2-phenoxy-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
-
2-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
-
3-acetylbenzo[d]oxazol-2(3H)-one
-
-
3-cyclohexyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
-
3-ethylbenzo[d]oxazole-2(3H)-thione
-
17% inhibition
3-hexanoylbenzo[d]oxazol-2(3H)-one
-
-
3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
-
3alpha-acetylpolyporenic acid A
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.040 mM
4-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)butan-1-one
-
-
benzyl 2-thioxobenzo[d]oxazol-3(2H)-carboxylate
-
-
beta1,4-galacto-oligosaccharides
-
partially sulfated and non-sulfated forms, IC50 values
-
Co2+
-
complete inhibition
D-isoascorbic acid
Streptomyces hyalurolyticus
-
strong inhibition
D-saccharic-1,4-lactone
Streptomyces hyalurolyticus
-
strong inhibition
dehydroascorbic acid
Streptomyces hyalurolyticus
-
-
dithiothreitol
5 mM, 30% inhibition
guanidine hydrochloride
strong inhibition, unfolding within 1 h
guanidine isothiocyanate
strong inhibition
hyaluronate
-
substrate inhibition above 7.5 mg/ml
L-arginine
strong inhibition
L-arginine methyl ester
strong inhibition
L-ascorbate
noncompetitive inhibition, inhibition kinetics, overview. Residues involved in the binding of L-ascorbate are confined to HylP135-308
L-ascorbic acid-6-hexadecanoate
lanostanoid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.051 mM
Li+
-
50 mM, 68% residual activity
methyl (9Z)-octadecenoate
methyl 2-sulfanylbenzo[d]oxazole-5-carboxylate
-
27% inhibition
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
-
-
N-(3-phenylpropionyl)-benzoxazole-2-thione
-
-
N-(3-phenylpropionyl)benzoxazole-2-thione
-
-
N-bromosuccinimide
5 mM, slight inhibition
N-ethylmaleimide
5 mM, slight inhibition
NaCl
slight inhibition, wild-type and mutant enzymes
Ni2+
-
complete inhibition
p-chloromercuribenzoate
5 mM, 30% inhibition
partially sulfated neomycin
-
the non-sulfated neomycin is not inhibitory
-
partially sulfated planteose
-
the non-sulfated planteose is not inhibitory, IC50 is 0.015 mM
partially sulfated verbascose
-
2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.030 mM and 0.001 mM
-
polyporenic acid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0125 mM
saccharic acid
Streptomyces hyalurolyticus
-
-
sulfated 2-hydroxyphenyl monolactobioside
-
IC50 is 0.35 mM
sulfated hydroquinone galactoside
-
IC50 is 0.080 mM
Tetranitromethane
-
inactivation, tyrosine-specific reagent
Triton X-100
-
weak inhibition
(13Z)-docos-13-enoic acid
-
strong inhibition
(13Z)-docos-13-enoic acid
Streptomyces hyalurolytics
-
weak inhibition
arachidic acid
-
weak inhibition
arachidic acid
Streptomyces hyalurolytics
-
weak inhibition
behenic acid
-
weak inhibition
behenic acid
Streptomyces hyalurolytics
-
weak inhibition
Ca2+
slight inhibition by 30% unfolding of the enzyme by ion binding
Ca2+
interacts with the collagenous Gly-X-Y motif of the enzyme, activates up to 20 mM, but inhibits at higher concentrations, inactivation above 50 mM
capric acid
-
weak inhibition
capric acid
Streptomyces hyalurolytics
-
weak inhibition
Cu2+
-
50 mM, no residual activity
Cu2+
-
complete inhibition
EDTA
-
5 mM, 84% residual activity
eicosadienoic acid
-
strong inhibition
eicosadienoic acid
Streptomyces hyalurolytics
-
weak inhibition
eicosanoic acid
-
strong inhibition
eicosanoic acid
Streptomyces hyalurolytics
-
weak inhibition
eicosapentaenoic acid
-
strong inhibition
eicosapentaenoic acid
Streptomyces hyalurolytics
-
weak inhibition
eicosatetraenoic acid
-
strong inhibition
eicosatetraenoic acid
Streptomyces hyalurolytics
-
weak inhibition
eicosatrienoic acid
-
strong inhibition
eicosatrienoic acid
Streptomyces hyalurolytics
-
weak inhibition
elaidic acid
-
-
elaidic acid
Streptomyces hyalurolytics
-
weak inhibition
iodoacetate
5 mM, slight inhibition
iodoacetate
-
10 mM, complete inhibition
L-ascorbic acid
-
-
L-ascorbic acid
i.e. vitamin C, reversible, competitive, one molecule binds to the active site of all 3 catalytic positions, interacts with enzyme residues R243, N290, W292, Y408, R462, R466, and N580, inhibits the invasion and spreading of the bacterium in tissues in vivo
L-ascorbic acid
Streptomyces hyalurolyticus
-
strong inhibition
L-ascorbic acid-6-hexadecanoate
-
-
L-ascorbic acid-6-hexadecanoate
-
lauric acid
-
weak inhibition
lauric acid
Streptomyces hyalurolytics
-
weak inhibition
linoleic acid
-
-
linoleic acid
Streptomyces hyalurolytics
-
weak inhibition
linolenic acid
-
-
linolenic acid
Streptomyces hyalurolytics
-
weak inhibition
methyl (9Z)-octadecenoate
-
-
methyl (9Z)-octadecenoate
Streptomyces hyalurolytics
-
weak inhibition
Mg2+
-
50 mM, 68% residual activity
Mg2+
slight inhibition by 30% unfolding of the enzyme by ion binding
myristic acid
-
weak inhibition
myristic acid
Streptomyces hyalurolytics
-
weak inhibition
myristoleic acid
-
-
myristoleic acid
Streptomyces hyalurolytics
-
weak inhibition
nervonic acid
-
strong inhibition
nervonic acid
Streptomyces hyalurolytics
-
weak inhibition
oleic acid
-
-
oleic acid
Streptomyces hyalurolytics
-
weak inhibition
palmitic acid
-
weak inhibition
palmitic acid
Streptomyces hyalurolytics
-
weak inhibition
palmitoleic acid
-
-
palmitoleic acid
Streptomyces hyalurolytics
-
weak inhibition
petroselinic acid
-
strong inhibition
petroselinic acid
Streptomyces hyalurolytics
-
weak inhibition
ricinoleic acid
-
-
ricinoleic acid
Streptomyces hyalurolytics
-
weak inhibition
SDS
-
5 mM, 4.6% residual activity
SDS
-
complete inhibition
stearic acid
-
weak inhibition
stearic acid
Streptomyces hyalurolytics
-
weak inhibition
Tween 80
-
5 mM, 84% residual activity
Tween 80
-
weak inhibition
vaccenic acid
-
strong inhibition
vaccenic acid
Streptomyces hyalurolytics
-
weak inhibition
Zn2+
-
-
additional information
-
inhibition curves, overview
-
additional information
structure-based design of bacterial hyaluronan lyase inhibitors, combinatorial chemistry database and crystal structure, method, overview
-
additional information
-
development of structure-based 1-acylated benzimidazole-2-thiones and benzoxazole-2-thiones inhibitors, using the crystal structure of Streptococcus pneumoniae Hyal, overview. Except for N-(3-phenylpropionyl)benzoxazole-2-thione, other N-acylated benzimidazoles and benzoxazoles are just as active at pH 7.4, but not at pH 5.0. The compounds show a binding mode characterized by interactions with residues in the catalytic site and with a hydrophobic patch, overview. No inhibition by 3-hexanoylbenzo[d]oxazol-2(3H)-one. Inhibition at pH 5.0, structure-activity relationships, overview
-
additional information
not inhibited by ascorbic acid at concentration up to 20 mM
-
additional information
no inhibition and conformational change induced by NaCl
-
additional information
-
no inhibition and conformational change induced by NaCl
-
additional information
IC50 for 1,3-diacetylbenzimidazole-2-thione is above 0.1 mM
-
additional information
-
IC50 for 1,3-diacetylbenzimidazole-2-thione is above 0.1 mM
-
additional information
Streptomyces hyalurolyticus
-
poor inhibitors are alpha-D-glucoheptonic-gamma-lactone, L-gulonic-gamma-lactone, D-ribonic-gamma-lactone, and D-gluconic-gamma-lactone
-
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A425K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
A487S
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
D170A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D170E
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
D373H
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D373H/K466Y/D478Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D432A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
D473E
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D473G
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D478Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D494T
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
D494T/K466Y
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
D537A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
E366S
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E366S/G367R
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
E440V
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, slightly reduced activity compared to the wild-type enzyme
G367R
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
G434A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, slightly reduced activity compared to the wild-type enzyme
G541A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H479A
-
site-directed mutagenesis, inactive mutant
H479G
-
site-directed mutagenesis, inactive mutant
I544D
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
K437A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
K437A/R542A
-
site-directed mutagenesis, mutation of residues in the putative EF hand motif, reduced activity compared to the wild-type enzyme
K466Y
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
K466Y/D478Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K466Y/D478Q/K725L/T726W
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K725L/T726W
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
K861E
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
M659G/D661K
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
M659G/D661K/K725L/T726W
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
N312A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
N370A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
N429A
-
site-directed mutagenesis, inactive mutant
N660A
-
site-directed mutagenesis, inactive mutant
R321L/R322Q
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
R380Q
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
R380Q/A478S
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R540A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
R542A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
R546A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, reduced activity compared to the wild-type enzyme
S539A
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, unaltered activity compared to the wild-type enzyme
S545V
-
site-directed mutagenesis, mutation of a residue in the putative EF hand motif, slightly reduced activity compared to the wild-type enzyme
W371A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W371A/W372A
-
site-directed mutagenesis, inactive mutant
W372A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y484F
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Y488F
-
site-directed mutagenesis, inactive mutant
Y488L
-
site-directed mutagenesis, inactive mutant
Y488T
-
site-directed mutagenesis, inactive mutant
D171A
catalytic mutant, 8% activity
Y183A
catalytic mutant, 13% activity
F343V
site-directed mutagensis, residue of the hydrophobic patch involved in substrate positioning during catalysis, reduced activity, crystallization for structure determination
R462A
modeling of site directed mutagenesis simulations of R462A and R462Q. The energetic profiles for the reaction processes are essentially the same as that in wild type enzyme, but the mutation accelerates the overall enzymatic activity. R462A can reduce the barrier height by about 2.8 kcal/mol. The positive charge on the R462 guanidino side chain group plays a negative role in the catalysis
R462Q
modeling of site directed mutagenesis simulations of R462A and R462Q. The energetic profiles for the reaction processes are essentially the same as that in wild type enzyme, but the mutation accelerates the overall enzymatic activity. R462Q can reduce the barrier height by about 2.9 kcal/mol. The positive charge on the R462 guanidino side chain group plays a negative role in the catalysis
W291A/W292A
site-directed mutagensis, residues of the hydrophobic patch involved in substrate positioning during catalysis, inactive mutant, crystallization for structure determination
W291A/W292A/F343V
site-directed mutagensis, residues of the hydrophobic patch involved in substrate positioning during catalysis, inactive mutant, crystallization for structure determination
W292A
site-directed mutagensis, residue of the hydrophobic patch involved in substrate positioning during catalysis, highly reduced activity, crystallization for structure determination
W292A/F343V
site-directed mutagensis, residues of the hydrophobic patch involved in substrate positioning during catalysis, highly reduced activity, crystallization for structure determination
M179V/M181V
-
mutations in the hot spot region of HylP, lead to fibrillation with the seeding of prefibrils
V147A
-
mutation in the hot spot region, abolishes fibril formation in HylP2
D170T
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q295E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W19F
site-directed mutagenesis, denaturation profile with guanidinium hydrochloride is similar to the wild-type enzyme
Y182F
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y298F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H399A
-
site-directed mutagenesis, highly reduced activity compared to wild-type enzyme
H399A
-
the mutant enzyme shows 12% of wild-type enzyme activity
N349A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
N349A
-
the mutant enzyme shows 6% of wild-type enzyme activity
N580G
-
site-directed mutagenesis, slightly increased activity compared to wild-type enzyme
N580G
-
the mutant enzyme shows 115% of wild-type enzyme activity
R243V
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R243V
-
the mutant enzyme shows 67% of wild-type enzyme activity
Y408F
-
site-directed mutagenesis, inactive mutant
Y408F
-
enzyme substrate complex structure determination by crystallization
Y408F
-
the mutant enzyme is inactive
V199D
gain of enzymatic activity from a previously inactive protein, numbering based on the sequence of HylA from strain 10403 (M-22)
V199D
-
gain of enzymatic activity from a previously inactive protein, numbering based on the sequence of HylA from strain 10403 (M-22)
-
V199D
mutant and wild-type protein have no enzymatic activity, numbering based on the sequence of HylA from strain 10403 (M-22)
V199D
-
mutant and wild-type protein have no enzymatic activity, numbering based on the sequence of HylA from strain 10403 (M-22)
-
additional information
-
construction of Hyal3 null mutants
additional information
-
inactivation of gene hysA by insertion of ermC, encoding the erythromycin determinant, from plasmid pE194 resulting in mutant strains HL-6, HL-13T, and HL-16T, determination of virulence and pathogenicity of wild-type strain 8325-4, and mutant strains HL-6, HL-13T, and HL-16T, WA250, deficient in regulator agr, and PC1839, deficient in regulator sar, in mice, overview
additional information
-
inactivation of gene hysA by insertion of ermC, encoding the erythromycin determinant, from plasmid pE194 resulting in mutant strains HL-6, HL-13T, and HL-16T, determination of virulence and pathogenicity of wild-type strain 8325-4, and mutant strains HL-6, HL-13T, and HL-16T, WA250, deficient in regulator agr, and PC1839, deficient in regulator sar, in mice, overview
-
additional information
-
mutation of the catalytic residues Asn429, His479, and Tyr488 inactivates the enzyme
additional information
construction of a fully active truncated enzyme form composed of the catalytic and C-terminal domains
additional information
-
construction of a fully active truncated enzyme form composed of the catalytic and C-terminal domains
additional information
-
C-terminal domain swapped chimeras of SpnHL and SagHL, modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid)
additional information
-
N-terminal swapped chimeras between phage hyaluronan lyases HylP and HylP2, i.e. N-HylP2-C-HylP and N-HylP-C-HylP2 or HylP do not form fibrils at acidic pH. Seeding of prefibrils of HylP2 recompenses nucleation and leads to fibrillation in N-HylP-C-HylP2
additional information
construction of truncated mutants hylp255e1113 and hylp390e1113, HylP enzyme without internal Gly-X-Y motif
additional information
-
construction of truncated mutants hylp255e1113 and hylp390e1113, HylP enzyme without internal Gly-X-Y motif
additional information
construction of an enzyme deficient strain by allelic relacement knockout of serotype 7
additional information
-
construction of an enzyme deficient strain by allelic relacement knockout of serotype 7
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Ozegowski, J.H.; Gerlach, D.; Khler, W.
Reinigung und Charakterisierung von Streptokokken-Hyaluronatlyase
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg.
249
310-322
1981
Streptococcus dysgalactiae subsp. equisimilis
-
brenda
Ingham, E.; Holland, K.T.; Gowland, G.; Cunliffe, W.J.
Purification and partial characterization of hyaluronate lyase (EC 4.2.2.1) from Propionibacterium acnes
J. Gen. Microbiol.
115
411-418
1979
Cutibacterium acnes
brenda
Hill, J.
Purification and properties of streptococcal hyaluronate lyase
Infect. Immun.
14
726-735
1976
Streptococcus sp.
brenda
Abramson, C.
Staphylococcal hyaluronate lyase
Contrib. Microbiol. Immunol.
1
376-389
1973
Staphylococcus aureus
brenda
Rautela, G.S.; Abramson, C.
Crystallization and partial characterization of Staphylococcus aureus hyaluronate lyase
Arch. Biochem. Biophys.
158
687-694
1973
Staphylococcus aureus, Staphylococcus aureus 1801
brenda
Gerlach, D.; Khler, W.
Hyaluronatlyase von Streptococcus pyogenes. II. Charakterisierung der Hyaluronatlyase (EC 4.2.99.1)
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg.
221
296-302
1972
Streptococcus pyogenes
-
brenda
Gerlach, D.; Khler, W.
Hyaluronatlyase von Streptococcus pyogenes. I. Bildung und Isolierung
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg.
221
166-172
1972
Streptococcus pyogenes
-
brenda
Vesterberg, O.
Studies on extracellular proteins from Staphylococcus aureus. 3. Investigations on the heterogeneity of hyaluronate lyase using the method of isoelectric focusing
Biochim. Biophys. Acta
168
218-227
1968
Staphylococcus aureus, Staphylococcus aureus M18
brenda
Abramson, C.; Friedman, H.
Staphylococcal hyaluronate lyase: purification and characterization studies
J. Bacteriol.
96
886-892
1968
Staphylococcus aureus, Staphylococcus aureus AEMC 1801
brenda
Arvidson, S.O.
Extracellular enzymes from Staphylococcus aureus
Staphylococci and Staphylococcal infections (Easmon, C. S. F. ; Adlam, C. , ed. )
2
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1983
Staphylococcus aureus
-
brenda
Bautista, J.; Chico, E.; Machado, A.
Effects of discharged fraction in repeated batch culture for hyaluronate lyase production
J. Ferment. Technol.
64
419-424
1986
Streptococcus dysgalactiae subsp. equisimilis, Streptococcus dysgalactiae subsp. equisimilis SHL-03
-
brenda
Gase, K.; Ozegowski, J.; Malke, H.
The Streptococcus agalactiae hylB gene encoding hyaluronate lyase: completion of the sequence and expression analysis
Biochim. Biophys. Acta
1398
86-98
1998
Streptococcus agalactiae, Streptococcus agalactiae 4755
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Cloning and sequencing of the hyaluronate lyase gene from Propionibacterium acnes
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43
315-321
1997
Cutibacterium acnes
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Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase
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121
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1998
Streptococcus pneumoniae
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Expression and purification of Streptococcus pneumoniae hyaluronate lyase from Escherichia coli
Protein Expr. Purif.
13
83-89
1998
Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae
brenda
Pritchard, D.G.; Lin, B.; Willingham, T.R.; Baker, J.R.
Characterization of the group B streptococcal hyaluronate lyase
Arch. Biochem. Biophys.
315
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1994
Streptococcus sp.
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Effects of oxygen concentration on biomass production, maximum specific growth rate and extracellular enzyme production by three species of cutaneous propionibacteria grown in continuous culture
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129
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1983
Cutibacterium acnes, Cutibacterium granulosum
brenda
Suzuki, K.; Terasaki, Y.; Uyeda, M.
Inhibition of hyaluronidases and chondroitinases by fatty acids
J. Enzyme Inhib. Med. Chem.
17
183-186
2002
Streptococcus dysgalactiae, Streptomyces hyalurolytics
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Okorukwu, O.; Vercruysse, K.P.
Effects of ascorbic acid and analogs on the activity of testicular hyaluronidase and hyaluronan lyase on hyaluronan
J. Enzyme Inhib. Med. Chem.
18
377-382
2003
Streptomyces hyalurolyticus
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de Assis, C.M.; Gandra, R.F.; Gambale, W.; Shimizu, M.T.; Paula, C.R.
Biosynthesis of chondroitinase and hyaluronidase by different strains of Paracoccidioides brasiliensis
J. Med. Microbiol.
52
479-481
2003
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brenda
Jedrzejas, M.J.; Chantalat, L.
Structural studies of streptococcus agalactiae hyaluronate lyase
Acta Crystallogr. Sect. D
56
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2000
Streptococcus agalactiae
brenda
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Action pattern and substrate specificity of the hyaluronan lyase from group B streptococci
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348
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2000
Streptococcus sp.
-
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Baker, J.R.; Dong, S.; Pritchard, D.G.
The hyaluronan lyase of Streptococcus pyogenes bacteriophage H4489A
Biochem. J.
365
317-322
2002
Streptococcus pyogenes phage H4489A
brenda
Li, S.; Kelly, S.J.; Lamani, E.; Ferraroni, M.; Jedrzejas, M.J.
Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase
EMBO J.
19
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Streptococcus pneumoniae
brenda
Oettl, M.; Hoechstetter, J.; Asen, I.; Bernhardt, G.; Buschauer, A.
Comparative characterization of bovine testicular hyaluronidase and a hyaluronate lyase from Streptococcus agalactiae in pharmaceutical preparations
Eur. J. Pharm. Sci.
18
267-277
2003
Streptococcus agalactiae
brenda
Hynes, W.L.; Walton, S.L.
Hyaluronidases of Gram-positive bacteria
FEMS Microbiol. Lett.
183
201-207
2000
Aeromonas sp., Porphyromonas asaccharolytica, Bacteroides fragilis, Prevotella melaninogenica, Bacteroides ovatus, Phocaeicola vulgatus, Candida albicans, Pichia kudriavzevii, Meyerozyma guilliermondii, Candida parapsilosis, Candida tropicalis, Clostridium chauvoei, Clostridioides difficile, Fusobacterium mortiferum, Cutibacterium granulosum, Streptococcus dysgalactiae, Streptococcus pyogenes, Streptococcus uberis, Streptomyces coelicolor, Treponema pallidum, Streptococcus equi, Clostridium septicum, Treponema pallidum subsp. pertenue, Streptococcus intermedius, Streptococcus constellatus, Staphylococcus hyicus, Streptomyces hyalurolyticus, Streptococcus agalactiae (O86478), Cutibacterium acnes (P0CZ01), Clostridium perfringens (P26831), Streptococcus pneumoniae (Q54873), Staphylococcus aureus (Q59801), Streptomyces griseus (Q9WXL3)
brenda
Kelly, S.J.; Taylor, K.B.; Li, S.; Jedrzejas, M.J.
Kinetic properties of Streptococcus pneumoniae hyaluronate lyase
Glycobiology
11
297-304
2001
Streptococcus pneumoniae
brenda
Suzuki, A.; Toyoda, H.; Toida, T.; Imanari, T.
Preparation and inhibitory activity on hyaluronidase of fully O-sulfated hyaluro-oligosaccharides
Glycobiology
11
57-64
2001
Streptomyces hyalurolyticus
brenda
Li, S.; Taylor, K.B.; Kelly, S.J.; Jedrzejas, M.J.
Vitamin C inhibits the enzymatic activity of Streptococcus pneumoniae hyaluronate lyase
J. Biol. Chem.
276
15125-15130
2001
Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae
brenda
Li, S.; Jedrzejas, M.J.
Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase
J. Biol. Chem.
276
41407-41416
2001
Streptococcus agalactiae (Q53591), Streptococcus agalactiae
brenda
Jedrzejas, M.J.; Mello, L.V.; de Groot, B.L.; Li, S.
Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. Structures of complexes with the substrate
J. Biol. Chem.
277
28287-28297
2002
Streptococcus pneumoniae
brenda
Mello, L.V.; De Groot, B.L.; Li, S.; Jedrzejas, M.J.
Structure and flexibility of Streptococcus agalactiae hyaluronate lyase complex with its substrate. Insights into the mechanism of processive degradation of hyaluronan
J. Biol. Chem.
277
36678-36688
2002
Streptococcus agalactiae (Q53591), Streptococcus agalactiae
brenda
Akhtar, M.S.; Bhakuni, V.
Streptococcus pneumoniae hyaluronate lyase contains two non-cooperative independent folding/unfolding structural domains: characterization of functional domain and inhibitors of enzyme
J. Biol. Chem.
278
25509-25516
2003
Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae
brenda
Nukui, M.; Taylor, K.B.; McPherson, D.T.; Shigenaga, M.K.; Jedrzejas, M.J.
The function of hydrophobic residues in the catalytic cleft of Streptococcus pneumoniae hyaluronate lyase. Kinetic characterization of mutant enzyme forms
J. Biol. Chem.
278
3079-3088
2003
Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae
brenda
Rigden, D.J.; Jedrzejas, M.J.
Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action
J. Biol. Chem.
278
50596-50606
2003
Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae
brenda
Ponnuraj, K.; Jedrzejas, M.J.
Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution
J. Mol. Biol.
299
885-895
2000
Streptococcus pneumoniae
brenda
Pritchard, D.G.; Trent, J.O.; Zhang, P.; Egan, M.L.; Baker, J.R.
Characterization of the active site of group B streptococcal hyaluronan lyase
Proteins Struct. Funct. Genet.
40
126-134
2000
Streptococcus agalactiae
brenda
Maccari, F.; Tripodi, F.; Volpi, N.
High-performance capillary electrophoresis separation of hyaluronan oligosaccharides produced by Streptomyces hyalurolyticus hyaluronate lyase
Carbohydr. Polym.
56
55-63
2004
Streptomyces hyalurolyticus
-
brenda
Kuehn, A.V.; Ozegowski, J.H.; Peschel, G.; Neubert, R.H.
Complementary exploration of the action pattern of hyaluronate lyase from Streptococcus agalactiae using capillary electrophoresis, gel-permeation chromatography and viscosimetric measurements
Carbohydr. Res.
339
2541-2547
2004
Streptococcus agalactiae, Streptococcus agalactiae 4755
brenda
Stern, R.; Jedrzejas, M.J.
Hyaluronidases: their genomics, structures, and mechanisms of action
Chem. Rev.
106
818-839
2006
Streptococcus agalactiae, Streptomyces hyalurolyticus, Streptococcus pyogenes phage H4489A, Streptococcus pneumoniae (Q54873)
brenda
Akhtar, M.S.; Bhakuni, V.
Streptococcus pneumoniae hyaluronate lyase: an overview
Curr. Sci.
86
285-295
2004
Streptococcus pneumoniae, Streptococcus agalactiae
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brenda
Wangun, H.V.K.; Berg, A.; Hertel, W.; Nkengfack, A.E.; Hertweck, C.
Anti-inflammatory and anti-hyaluronate lyase activities of lanostanoids from Piptoporus betulinus
J. Antibiot.
57
755-758
2004
Streptococcus agalactiae
brenda
King, S.J.; Allen, A.G.; Maskell, D.J.; Dowson, C.G.; Whatmore, A.M.
Distribution, genetic diversity, and variable expression of the gene encoding hyaluronate lyase within the Streptococcus suis population
J. Bacteriol.
186
4740-4747
2004
Streptococcus suis (Q6H8W8), Streptococcus suis (Q6H8W9), Streptococcus suis (Q6H8X0), Streptococcus suis (Q6H8X1), Streptococcus suis (Q6H8X2), Streptococcus suis (Q6H8X4), Streptococcus suis (Q6H8X5), Streptococcus suis (Q6H8X6), Streptococcus suis (Q6H8X7), Streptococcus suis (Q6H8X8), Streptococcus suis (Q6H8Y0), Streptococcus suis (Q6H8Y1), Streptococcus suis (Q6H8Y2), Streptococcus suis (Q6H8Y3), Streptococcus suis (Q6H8Y4), Streptococcus suis (Q8VLQ7), Streptococcus suis (Q8VLQ8), Streptococcus suis
brenda
Mishra, P.; Akhtar, M.S.; Bhakuni, V.
Unusual structural features of the bacteriophage-associated hyaluronate lyase (hylp2)
J. Biol. Chem.
281
7143-7150
2006
Streptococcus pyogenes phage H10403
brenda
Rigden, D.J.; Littlejohn, J.E.; Joshi, H.V.; de Groot, B.L.; Jedrzejas, M.J.
Alternate structural conformations of Streptococcus pneumoniae hyaluronan lyase: insights into enzyme flexibility and underlying molecular mechanism of action
J. Mol. Biol.
358
1165-1178
2006
Streptococcus agalactiae (Q53591), Streptococcus agalactiae, Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae
brenda
Allen, A.G.; Lindsay, H.; Seilly, D.; Bolitho, S.; Peters, S.E.; Maskell, D.J.
Identification and characterisation of hyaluronate lyase from Streptococcus suis
Microb. Pathog.
36
327-335
2004
Streptococcus suis (Q8VLQ8), Streptococcus suis
brenda
Makris, G.; Wright, J.D.; Ingham, E.; Holland, K.T.
The hyaluronate lyase of Staphylococcus aureus - a virulence factor?
Microbiology
150
2005-2013
2004
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
brenda
Salmen, S.; Hoechstetter, J.; Kaesbauer, C.; Paper, D.H.; Bernhardt, G.; Buschauer, A.
Sulphated oligosaccharides as inhibitors of hyaluronidases from bovine testis, bee venom and Streptococcus agalactiae
Planta Med.
71
727-732
2005
Streptococcus agalactiae, Streptococcus agalactiae 4755
brenda
Botzki, A.; Salmen, S.; Bernhardt, G.; Buschauer, A.; Dove, S.
Structure-based design of bacterial hyaluronan lyase inhibitors
QSAR Comb. Sci.
24
458-469
2005
Streptococcus agalactiae (Q53591)
-
brenda
Tufto, I.; Hansen, R.; Byberg, D.; Nygaard, K.H.; Tufto, J.; Davies, C.d.e.L.
The effect of collagenase and hyaluronidase on transient perfusion in human osteosarcoma xenografts grown orthotopically and in dorsal skinfold chambers
Anticancer Res.
27
1475-1481
2007
Bos taurus
brenda
Akhtar, M.S.; Bhakuni, V.
Role of ionic interactions and linker in the domain interaction and modulation of functional activity of hyaluronate lyases
Biochem. Biophys. Res. Commun.
353
286-292
2007
Streptococcus pneumoniae
brenda
Yang, P.; Lee, C.
Purification of recombinant hyaluronan lyase of Streptococcus pyogenes bacteriophage H4489A expressed in Escherichia coli and its application for the specific determination of hyaluronan concentration
Carbohydr. Polym.
65
159-164
2006
Streptococcus pyogenes phage H4489A
-
brenda
Taylor, T.H.; Elliott, T.; Colturato, L.F.; Straub, R.J.; Mitchell-Leef, D.; Nagy, Z.P.
Comparison of bovine- and recombinant human-derived hyaluronidase with regard to fertilization rates and embryo morphology in a sibling oocyte model: a prospective, blinded, randomized study
Fertil. Steril.
85
1544-1546
2006
Bos taurus, Homo sapiens
brenda
Rigden, D.J.; Botzki, A.; Nukui, M.; Mewbourne, R.B.; Lamani, E.; Braun, S.; von Angerer, E.; Bernhardt, G.; Dove, S.; Buschauer, A.; Jedrzejas, M.J.
Design of new benzoxazole-2-thione-derived inhibitors of Streptococcus pneumoniae hyaluronan lyase: structure of a complex with a 2-phenylindole
Glycobiology
16
757-765
2006
Streptococcus agalactiae, Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae, Streptococcus agalactiae 4755
brenda
Akhtar, M.S.; Krishnan, M.Y.; Bhakuni, V.
Insights into the mechanism of action of hyaluronate lyase: role of C-terminal domain and Ca2+ in the functional regulation of enzyme
J. Biol. Chem.
281
28336-28344
2006
Streptococcus agalactiae (Q53591), Streptococcus agalactiae
brenda
Harada, H.; Takahashi, M.
CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and -2
J. Biol. Chem.
282
5597-5607
2007
Homo sapiens (Q12794), Homo sapiens (Q12891)
brenda
Ganesh, S.; Gonzalez-Edick, M.; Gibbons, D.; Van Roey, M.; Jooss, K.
Intratumoral coadministration of hyaluronidase enzyme and oncolytic adenoviruses enhances virus potency in metastatic tumor models
Clin. Cancer Res.
14
3933-3941
2008
Homo sapiens
brenda
Ozegowski, J.H.; Presselt, N.; Haertl, A.; Bocker, T.; Saenger, J.; Schmidt, A.; Willing, K.; Mueller, P.J.
Anti-atherosclerotic effect of microbial hyaluronate lyase from group B streptococci
Pharmazie
63
601-605
2008
Streptococcus agalactiae (O86478), Streptococcus agalactiae
brenda
Mishra, P.; Bhakuni, V.
Self-assembly of bacteriophage-associated hyaluronate lyase (HYLP2) into an enzymatically active fibrillar film
J. Biol. Chem.
284
5240-5249
2009
Streptococcus pyogenes phage H10403
brenda
Hynes, W.; Johnson, C.; Stokes, M.
A single nucleotide mutation results in loss of enzymatic activity in the hyaluronate lyase gene of Streptococcus pyogenes
Microb. Pathog.
47
308-313
2009
Streptococcus pyogenes MGAS10750, Streptococcus pyogenes MGAS5005, Streptococcus pyogenes MGAS10270, Streptococcus pyogenes MGAS315, Streptococcus pyogenes str. Manfredo, Streptococcus pyogenes MGAS10394, Streptococcus pyogenes MGAS9429, Streptococcus pyogenes MGAS8232, Streptococcus pyogenes MGAS6180, Streptococcus pyogenes NZ131, Streptococcus pyogenes (A7XFU3), Streptococcus pyogenes (A7XFU4), Streptococcus pyogenes (A7XFV0), Streptococcus pyogenes (A7XFV1), Streptococcus pyogenes (Q9L7W9), Streptococcus pyogenes, Streptococcus pyogenes serotype M4 (A7XFU5), Streptococcus pyogenes serotype M4 (A7XFU6), Streptococcus pyogenes serotype M4 (A7XFV2), Streptococcus pyogenes serotype M4 (A7XFV5), Streptococcus pyogenes serotype M3 (A7XFU7), Streptococcus pyogenes serotype M3 (A7XFU8), Streptococcus pyogenes serotype M3 (A7XFU9), Streptococcus pyogenes serotype M3 (A7XFV3), Streptococcus pyogenes serotype M3 (A7XFV4), Streptococcus pyogenes serotype M3 (A7XFV6), Streptococcus pyogenes serotype M3 (A7XFV7), Streptococcus pyogenes serotype M1 (Q99ZX4), Streptococcus pyogenes serotype M3 94146 (A7XFV4), Streptococcus pyogenes serotype M3 350 (A7XFU8), Streptococcus pyogenes serotype M3 1020 (A7XFV6), Streptococcus pyogenes serotype M4 2397 (A7XFV5), Streptococcus pyogenes serotype M3 3779 (A7XFV7), Streptococcus pyogenes serotype M3 422 (A7XFU9), Streptococcus pyogenes serotype M1 SF370 (Q99ZX4), Streptococcus pyogenes serotype M4 4282 (A7XFV2), Streptococcus pyogenes serotype M4 445 (A7XFU6), Streptococcus pyogenes serotype M3 872 (A7XFV3), Streptococcus pyogenes serotype M4 4283 (A7XFU5), Streptococcus pyogenes serotype M3 1055 (A7XFU7)
brenda
Lindsay, A.M.; Zhang, M.; Mitchell, Z.; Holden, M.T.; Waller, A.S.; Sutcliffe, I.C.; Black, G.W.
The Streptococcus equi prophage-encoded protein SEQ2045 is a hyaluronan-specific hyaluronate lyase that is produced during equine infection
Microbiology
155
443-449
2009
Streptococcus equi subsp. equi 4047 (C0M9W4)
brenda
Joshi, H.; Jedrzejas, M.; De Groot, B.
Domain motions of hyaluronan lyase underlying processive hyaluronan translocation
Proteins
76
30-46
2009
Streptococcus pneumoniae
brenda
El-Safory, N.; Lee, G.; Lee, C.
Characterization of hyaluronate lyase from Streptococcus pyogenes bacteriophage H4489A
Carbohydr. Polym.
84
1182-1191
2011
Streptococcus pyogenes phage H4489A
brenda
Braun, S.; Botzki, A.; Salmen, S.; Textor, C.; Bernhardt, G.; Dove, S.; Buschauer, A.
Design of benzimidazole- and benzoxazole-2-thione derivatives as inhibitors of bacterial hyaluronan lyase
Eur. J. Med. Chem.
46
4419-4429
2011
Streptococcus agalactiae, Streptococcus agalactiae 4755
brenda
Reese, K.L.; Aravindan, R.G.; Griffiths, G.S.; Shao, M.; Wang, Y.; Galileo, D.S.; Atmuri, V.; Triggs-Raine, B.L.; Martin-Deleon, P.A.
Acidic hyaluronidase activity is present in mouse sperm and is reduced in the absence of SPAM1: evidence for a role for hyaluronidase 3 in mouse and human sperm
Mol. Reprod. Dev.
77
759-772
2010
Homo sapiens, Mus musculus
brenda
Khan, A.H.; Mohamed Omar, Y.M.; Kakar, M.A.; Bangulzai, N.
Crystallization and preliminary crystallographic analysis of recombinant hyaluronate lyase from Streptococcus suis
Acta Crystallogr. Sect. F
69
673-675
2013
Streptococcus suis
brenda
Singh, S.K.; Malhotra, S.; Akhtar, M.S.
Characterization of hyaluronic acid specific hyaluronate lyase (HylP) from Streptococcus pyogenes
Biochimie
102
203-210
2014
Streptococcus pyogenes phage H4489A (P15316), Streptococcus pyogenes phage H4489A
brenda
Zheng, M.; Zhang, H.; Xu, D.
Initial events in the degradation of hyaluronan catalyzed by hyaluronate lyase from Spectrococcus pneumoniae: QM/MM simulation
J. Phys. Chem. B
116
11166-11172
2012
Streptococcus pneumoniae
brenda
Zheng, M.; Xu, D.
Catalytic mechanism of hyaluronate lyase from Spectrococcus pneumonia: quantum mechanical/molecular mechanical and density functional theory studies
J. Phys. Chem. B
117
10161-10172
2013
Streptococcus pneumoniae
brenda
Zhu, C.; Zhang, J.; Li, L.; Zhang, J.; Jiang, Y.; Shen, Z.; Guan, H.; Jiang, X.
Purification and characterization of hyaluronate lyase from Arthrobacter globiformis A152
Appl. Biochem. Biotechnol.
182
216-228
2017
Arthrobacter globiformis, Arthrobacter globiformis A152
brenda
Haas, B.; Vaillancourt, K.; Bonifait, L.; Gottschalk, M.; Grenier, D.
Hyaluronate lyase activity of Streptococcus suis serotype 2 and modulatory effects of hyaluronic acid on the bacteriums virulence properties
BMC Res. Notes
8
722
2015
Streptococcus suis
brenda
Tao, L.; Song, F.; Xu, N.; Li, D.; Linhardt, R.J.; Zhang, Z.
New insights into the action of bacterial chondroitinase AC I and hyaluronidase on hyaluronic acid
Carbohydr. Polym.
158
85-92
2017
Pedobacter heparinus
brenda
Sun, X.; Wang, Z.; Bi, Y.; Wang, Y.; Liu, H.
Genetic and functional characterization of the hyaluronate lyase HylB and the beta-N-acetylglucosaminidase HylZ in Streptococcus zooepidemicus
Curr. Microbiol.
70
35-42
2015
Streptococcus equi subsp. zooepidemicus (W6E7E9), Streptococcus equi subsp. zooepidemicus
brenda
Li, F.; Xu, D.
Functional role of R462 in the degradation of hyaluronan catalyzed by hyaluronate lyase from Streptococcus pneumoniae
J. Mol. Model.
21
196
2015
Streptococcus pneumoniae (Q54873), Streptococcus pneumoniae
brenda
Kurata, A.; Matsumoto, M.; Kobayashi, T.; Deguchi, S.; Kishimoto, N.
Hyaluronate lyase of a deep-sea Bacillus niacini
Mar. Biotechnol.
17
277-284
2015
Neobacillus niacini (X5I0R2), Neobacillus niacini, Neobacillus niacini JAM F8 (X5I0R2)
brenda
Mai, V.Q.; Vo, T.T.; Meere, M.
Modelling hyaluronan degradation by streptococcus pneumoniae hyaluronate lyase
Mathr. Biosci.
303
126-138
2018
Streptococcus pneumoniae
brenda
Nazipi, S.; Stodkilde-Jorgensen, K.; Scavenius, C.; Brueggemann, H.
The skin bacterium Propionibacterium acnes employs two variants of hyaluronate lyase with distinct properties
Microorganisms
5
57
2017
Cutibacterium acnes
brenda
Kasparova, J.; Korecka, L.; Pepeliaev, S.; Bilkova, Z.; Smirnou, D.; Velebny, V.; Ceslova, L.
Magnetic macroporous bead cellulose functionalised with recombinant hyaluronan lyase for controllable hyaluronan fragmentation
Process Biochem.
72
105-111
2018
Streptococcus pneumoniae
-
brenda
Shukla, H.; Singh, S.; Singh, A.; Mitra, K.; Akhtar, M.
The C-terminus hot spot region helps in the fibril formation of bacteriophage-associated hyaluronate lyase (HylP2)
Sci. Rep.
5
14429
2015
Streptococcus pyogenes phage
brenda
Yusof, H.A.; Desa M, N.M.; Masri, S.N.; Malina, O.; Jamal, F.
Hyaluronatelyase production by Streptococcus pneumoniae isolated from patients and carriers
Trop. Biomed.
32
413-418
2015
Streptococcus pneumoniae
brenda