Literature summary for 4.2.2.1 extracted from

Jedrzejas, M.J.; Chantalat, L.
Structural studies of streptococcus agalactiae hyaluronate lyase (2000), Acta Crystallogr. Sect. D, 56, 460-463.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant 111 kDa and 92 kDa enzyme forms, hanging drop vapour diffusion method, equal volumes of 0.001-0.005 ml of protein solution and reservoir solution, the latter containing 0.1 M cacodylate, pH 6.0, 30 mM KSCN, various amount of PEG-monomethyl ether 5000, over 1 ml reservoir solution, precipitation with PEG monomethyl ether 5000 and potassium thiocyanate at room temperature, X-ray diffraction structure determination and analysis at 2.1 A resolution	Streptococcus agalactiae

Crystallization (Comment)

Organism

purified recombinant 111 kDa and 92 kDa enzyme forms, hanging drop vapour diffusion method, equal volumes of 0.001-0.005 ml of protein solution and reservoir solution, the latter containing 0.1 M cacodylate, pH 6.0, 30 mM KSCN, various amount of PEG-monomethyl ether 5000, over 1 ml reservoir solution, precipitation with PEG monomethyl ether 5000 and potassium thiocyanate at room temperature, X-ray diffraction structure determination and analysis at 2.1 A resolution

Streptococcus agalactiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
92000	-	autocatalytically processed enzyme, gel filtration	Streptococcus agalactiae
111000	-	pro-form, gel filtration	Streptococcus agalactiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Streptococcus agalactiae	the enzyme contributes to the invasive capacity of the pathogenic organism by degrading hyaluronan and chondroitin sulfates of the extracellular matrix of host tissues	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptococcus agalactiae	-	allele hylB3502	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	autocatalytic conversion to a smaller 92kDa active enzyme form, completely prevented by 2 mM EDTA	Streptococcus agalactiae

Reaction

Reaction	Comment	Organism	Reaction ID
[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	Streptococcus agalactiae	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3571	-	purified 92 kDa mature form	Streptococcus agalactiae
3680	-	purified 111 kDa pro-form	Streptococcus agalactiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
chondroitin sulfate	-	Streptococcus agalactiae	?	-	ir
hyaluronan	-	Streptococcus agalactiae	3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine	-	ir
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	Streptococcus agalactiae	?	-	?