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4.2.2.1: hyaluronate lyase

This is an abbreviated version!
For detailed information about hyaluronate lyase, go to the full flat file.

Word Map on EC 4.2.2.1

Reaction

[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

Synonyms

acidic hyase, bacterial HAse, bacterial hyaluronidase, bacterial spreading factor, bacteriophage-associated hyaluronate lyase, Cumulase, EC 4.2.99.1, GBS HA lyase, GBS hyase, glucuronoglycosaminoglycan lyase, h-SD, h-SH, HA lyase, HL, Hyal, Hyal-1, Hyal-2, HYAL1, Hyal2, HYAL3, hyaluronan lyase, hyaluronate lyase, hyaluronate lyase HylA, hyaluronate lyase HylP2, hyaluronidase, hyaluronidase 3, hyaluronidase SD, hyaluronidase SH, hyaluronidase-1, hyaluronidase-2, hyaluronoglucosaminidase-1, hyaluronoglucosaminidase-2, HYase, HylA7, hylB, hylB4755, HylP, Hylp2, LUCA-1, LUCA-2, lyase, glucuronoglycosaminoglycan, lyase, hyaluronate, More, mucinase, protein SEQ2045, rHuPH20, SagHL, SagHyal, spnHL, SpnHyal, spreading factor, SP_0314

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.1 hyaluronate lyase

Crystallization

Crystallization on EC 4.2.2.1 - hyaluronate lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme-hyaluronate hexasaccharide substrate complex, hanging drop vapour diffusion method, room temperature, in 10-50 mM hyaluronate hexasaccharide, 0.1 M sodium cacodylate, pH 6.0, 30 mM potassium thiocyanate, 30% PEG monomethyl ester 5000, several days, X-ray diffraction structure determination and analysis at 2.2 A resolution
purified free enzyme and enzyme-product complex, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
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
-
5 mg/ml Y408 mutant enzyme complexed with tetra- and hexasaccharide hyaluronan substrates, in 10 mM Tris-HCl, pH 7.4, 2 mM EDTA, 1 mM DL-dithiothreitol, against 100 mM sodium cacodylate, pH 6.0, 2.9 M ammonium sulfate, 5 mM EDTA, hanging drop vapour diffusion method, 0.002 ml equal volumes of protein and reservoir solution, 22°C, equilibration against 1 ml reservoir solution, several days, X-ray diffraction structure determination and analysis at 1.52-2.0 A resolution
-
crystal structure analysis
enzyme complexed with L-ascorbic acid, X-ray diffraction structure determination and analysis at 2.0 A resolution
enzyme-disaccharide complex, X-ray diffraction structure determination and analysis at 1.7 A resolution, structure modeling
-
enzyme-substrate complexes, wild-type enzyme and mutants H399A, and Y408F, each 5 mg/ml in 10 mM Tris-HCl, pH 7.4, 2 mM EDTA, hanging drop vapour diffusion method, equal volumes of protein, 50 mM chondroitin in 10 mM Tris-HCl solution, and reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.56 A resolution
hanging drop vapor diffusion method, 1-decyl-2-(4-sulfamoyloxyphenyl)-1-indol-6-yl sulfamate is co-crystallized in a complex with Streptococcus pneumoniae Hyal
mutant enzymes at 5.1-6.2 mg/ml concentration, hanging drop vapour diffusion method, equal volumes of protein and reservoir solutions, the latter containing 60-65% saturated ammonium sulfate, 0.2 M sodium chloride, 2% dioxane, 500 mM sodium citrate, pH 6.0, X-ray diffraction structure determination and analysis at 1.5-2.3 A resolution
purified recombinant fully active truncated enzyme form composed of the catalytic and C-terminal domains by two different method resulting in different crystal forms, 5 mg/ml protein in 10 mM Tris-HCl, pH 7.4, 150 mM NaCl, and 2 mM EDTA, hanging drop vapour diffusion method, mixing with an equal volume of reservoir solution containing 1. 30% PEG 2000 monomethyl ester, 0.1 M MES, pH 6.5, and 0.2 M ammonium sulfate, or 2. 70% w/v saturated malonic acid, pH 7.6, and 0.1 M sodium cacodylate, ph 6.6, several months, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular dynamic simulations
purified recombinant truncated wid-type enzyme and selenomethionine derivative, comprising residues Ala168-Ala893, in 3.5 M ammonium sulfate, 200 mM sodium cacodylate, pH 6.0, cryoprotection in 30% xylitol, heavy atom derivative X-ray diffraction structure determination and analysis at 1.56 A resolution
-
truncated 83000 Da functional form is cloned into the pET-21d vector
-
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, 0.001 ml of protein in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, 1 mM mercaptoethanol, and 1 mM EDTA, is mixed with 0.001 ml of reservoir solution, and equilibrated against 0.25 ml of reservoir solution, a few weeks, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular-replacement method
-