Information on EC 4.2.2.1 - hyaluronate lyase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
4.2.2.1
-
RECOMMENDED NAME
GeneOntology No.
hyaluronate lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
lyase mechanism, elimination process
Streptomyces hyalurolyticus
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
rapid elimination mechanism
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
catalytic mechanism, substrate binding, structure modeling, residues Tyr408, Asn349, and His399 are involved in catalysis and important
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
P26831
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
Q59634
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
O86478
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
Q9WXL3
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
Q53591
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
Asn349, His399, and Tyr408 are involved in catalysis, flexible, allosteric behavior of the enzyme, mechanism, active site structure and substrate binding and interactions, overview
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
catalytic mechanism, the flexibility of the enzyme structure is important, the beta-domain is involved in the progressive catalytic process, enzyme substrate interactions
Q53591
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
active site structure and substrate binding of wild-type and mutant enzymes with chondroitin, mode of action
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
enzyme-product interaction from crystal structure, catalytic mechanism, interaction with substrate binding site, Tyr408, Asn349, and His399 are involved
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
His479 is critical for activity, active site structure, mechanism
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
mechanism of hyaluronan degradation, random endolytic action pattern, overview
Streptomyces hyalurolyticus
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
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
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
catalytic reaction mechanism and structural requirements, catalytic residues are Asn349, His399, and Tyr408
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408; catalytic residues are Asn349, His399, and Tyr408
Q6H8W8, Q6H8W9, Q6H8X0, Q6H8X1, Q6H8X2, Q6H8X4, Q6H8X5, Q6H8X6, Q6H8X7, Q6H8X8, Q6H8Y0, Q6H8Y1, Q6H8Y2, Q6H8Y3, Q6H8Y4, Q8VLQ7, Q8VLQ8
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
active site structure
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
active site structure and hydrophobic patch, molecular mechanism, enzyme flexibility and structural requirements
-
Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
catalytic residues are Asn349, His399, and Tyr408
Q8VLQ8
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-elimination
-
-
beta-elimination
-
termed proton acceptance and donation
elimination
-
-
-
-
elimination
-
-
elimination
O86478
-
SYSTEMATIC NAME
IUBMB Comments
hyaluronate lyase
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
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acidic hyase
-
-
bacterial HAse
Streptomyces hyalurolyticus
-
-
bacterial hyaluronidase
Streptomyces hyalurolyticus
-
-
bacterial spreading factor
-
-
bacteriophage-associated hyaluronate lyase
-
-
Cumulase
-
-
EC 4.2.99.1
-
-
formerly
-
GBS HA lyase
-
-
GBS HA lyase
Streptococcus agalactiae 4755
-
-
-
GBS hyase
-
-
glucuronoglycosaminoglycan lyase
-
-
-
-
h-SH
Streptomyces hyalurolytics
-
-
Hyal
Streptococcus agalactiae 4755
-
-
-
Hyal-1
Q12794
-
Hyal-2
Q12891
-
HYAL1
Q12794
-
Hyal2
Q12891
-
hyaluronan lyase
-
-
hyaluronan lyase
Streptococcus agalactiae 4755
-
-
-
hyaluronan lyase
-
-
hyaluronan lyase
Streptomyces hyalurolyticus
-
-
hyaluronate lyase
O86478
-
hyaluronate lyase
C0M9W4
-
hyaluronate lyase HylA
A7XFU3, A7XFU4, A7XFV0, A7XFV1, Q9L7W9
-
hyaluronate lyase HylA
Q99ZX4
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M1 SF370
Q99ZX4
-
-
hyaluronate lyase HylA
A7XFU7, A7XFU8, A7XFU9, A7XFV3, A7XFV4, A7XFV6, A7XFV7
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M3 1020
A7XFV6
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M3 1055
A7XFU7
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M3 350
A7XFU8
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M3 3779
A7XFV7
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M3 422
A7XFU9
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M3 872
A7XFV3
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M3 94146
A7XFV4
-
-
hyaluronate lyase HylA
A7XFU5, A7XFU6, A7XFV2, A7XFV5
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M4 2397
A7XFV5
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M4 4282
A7XFV2
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M4 4283
A7XFU5
-
-
hyaluronate lyase HylA
Streptococcus pyogenes serotype M4 445
A7XFU6
-
-
hyaluronate lyase HylA
-
-
hyaluronate lyase HylP2
-
-
hyaluronidase
-
-
-
-
hyaluronidase
-
-
hyaluronidase
Q6H8W8, Q6H8W9, Q6H8X0, Q6H8X1, Q6H8X2, Q6H8X4, Q6H8X5, Q6H8X6, Q6H8X7, Q6H8X8, Q6H8Y0, Q6H8Y1, Q6H8Y2, Q6H8Y3, Q6H8Y4
-
hyaluronidase
Q8VLQ8
-
hyaluronidase
Streptomyces hyalurolyticus
-
-
hyaluronidase 3
-
-
hyaluronidase SH
Streptomyces hyalurolytics
-
-
hyaluronidase-1
Q12794
-
hyaluronidase-2
Q12891
-
hyaluronoglucosaminidase-1
Q12794
-
hyaluronoglucosaminidase-2
Q12891
-
HYase
-
-
-
-
HYase
-
-
HylA7
Q8VLQ8
-
hylB4755
Streptococcus agalactiae 4755
-
-
-
LUCA-1
Q12794
-
LUCA-2
Q12891
-
lyase, glucuronoglycosaminoglycan
-
-
-
-
mucinase
-
-
-
-
protein SEQ2045
C0M9W4
-
Q59801 {SwissProt}
-
-
SagHyal
Streptococcus agalactiae 4755
-
-
-
spreading factor
-
-
-
-
spreading factor
-
-
spreading factor
Q54873
-
lyase, hyaluronate
-
-
-
-
additional information
-
from commercial pharmaceutical preparations Neopermease and Hylase Dessau
additional information
-
the enzyme belongs to the polysaccharide lyase family 8
additional information
-
the enzyme belongs to the CAZY polysaccharide lyase family 16
CAS REGISTRY NUMBER
COMMENTARY
37259-53-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bacteroides melaninogenicus
-
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
recombinant hyaluronidase enzyme (rHuPH20)
-
-
Manually annotated by BRENDA team
several different isozymes
-
-
Manually annotated by BRENDA team
several different isozymes
-
-
Manually annotated by BRENDA team
different strains isolated from different host organisms, e.g. human, penguin, armadillo, and from dog food
-
-
Manually annotated by BRENDA team
-
Q59634
SwissProt
Manually annotated by BRENDA team
strain 1801
-
-
Manually annotated by BRENDA team
strain 8325-4, gene hysA
-
-
Manually annotated by BRENDA team
strain M18
-
-
Manually annotated by BRENDA team
Staphylococcus aureus 1801
strain 1801
-
-
Manually annotated by BRENDA team
Staphylococcus aureus 8325-4
strain 8325-4, gene hysA
-
-
Manually annotated by BRENDA team
Staphylococcus aureus AEMC 1801
AEMC 1801
-
-
Manually annotated by BRENDA team
Staphylococcus aureus M18
strain M18
-
-
Manually annotated by BRENDA team
allele hylB3502
-
-
Manually annotated by BRENDA team
gene hylB3502, strain 3502
SwissProt
Manually annotated by BRENDA team
serotype III GBS strain 3502
-
-
Manually annotated by BRENDA team
strain 4755
SwissProt
Manually annotated by BRENDA team
strain 4755, gene hylB4755
-
-
Manually annotated by BRENDA team
strain group B
SwissProt
Manually annotated by BRENDA team
strains 3502, gene hyl3502, and 4755, gene hyl4755
SwissProt
Manually annotated by BRENDA team
Streptococcus agalactiae 4755
-
-
-
Manually annotated by BRENDA team
Streptococcus agalactiae 4755
strain 4755
-
-
Manually annotated by BRENDA team
Streptococcus agalactiae 4755
strain 4755
SwissProt
Manually annotated by BRENDA team
Streptococcus agalactiae 4755
strain 4755, gene hylB4755
-
-
Manually annotated by BRENDA team
Streptococcus dysgalactiae subsp. equisimilis SHL-03
strain SHL-03
-
-
Manually annotated by BRENDA team
group A; out of 40 strains only the types 4, 22 and 24 form large amount of the enzyme. Small activities are also demostrated with the types 5, 19, 25 and 28
-
-
Manually annotated by BRENDA team
group A; type 24
-
-
Manually annotated by BRENDA team
M-22 strain 3200
UniProt
Manually annotated by BRENDA team
M-22 strain 437
UniProt
Manually annotated by BRENDA team
M-22 strain 4786
UniProt
Manually annotated by BRENDA team
M-22 strain 6219
UniProt
Manually annotated by BRENDA team
M-22, strain 10403
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M1 SF370
strain SF370
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 1020
strain 1020
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 1055
strain 1055
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 350
strain 350
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 3779
strain 3779
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 422
strain 422
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 872
strain 872
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M3 94146
strain 94146
UniProt
Manually annotated by BRENDA team
strain 4283
A7XFU5
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 2397
strain 2397
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 4282
strain 4282
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 4283
strain 4283
A7XFU5
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes serotype M4 445
strain 445
UniProt
Manually annotated by BRENDA team
group A type 4
-
-
Manually annotated by BRENDA team
serotype III, strain 3502
-
-
Manually annotated by BRENDA team
hyaluronidase fragment; gene hylA, 309 isolates of different serotypes, geographic sources, and clinical backgrounds
SwissProt
Manually annotated by BRENDA team
hyaluronidase precursor; gene hylA, 309 isolates of different serotypes, geographic sources, and clinical backgrounds
SwissProt
Manually annotated by BRENDA team
hyaluronidase precursor; gene hylAP1/7, serotype 7
SwissProt
Manually annotated by BRENDA team
capsular and acapsular phenotype, contains 2 forms: a extracellular and a bacteriophage enzyme
-
-
Manually annotated by BRENDA team
Streptomyces hyalurolytics
-
-
-
Manually annotated by BRENDA team
Streptomyces hyalurolyticus
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
Hyal3 null sperm shows delayed cumulus penetration and reduced acrosomal exocytosis, but full fertility
physiological function
C0M9W4
produced during infection of horses
physiological function
-
hyaluronan lyases degrade hyaluronan, an important component of the extracellular matrix, and are involved in microbial spread
physiological function
-
in general, neutral-active or reproductive hyaluronidases, i.e. hyases, exemplified by sperm adhesion molecule 1, SPAM1, are responsible for hyaluronan digestion in the egg vestments and for sperm-zona binding. Presence of HYAL3 in human sperm where it contributes to hyase activity at pH 3, 4 and 7 as well as to cumulus penetration and the induction of the acrosome reaction
physiological function
-
in general, neutral-active or reproductive hyaluronidases, i.e. hyases, exemplified by sperm adhesion molecule 1, SPAM1, are responsible for hyaluronan digestion in the egg vestments and for sperm-zona binding, but murine SPAM1 has acidic activity. Presence of HYAL3 in mouse sperm where it contributes to hyase activity at pH 3, 4 and 7 as well as to cumulus penetration and the induction of the acrosome reaction
physiological function
Streptococcus agalactiae 4755
-
hyaluronan lyases degrade hyaluronan, an important component of the extracellular matrix, and are involved in microbial spread
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chondroitin
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-galactosamine
show the reaction diagram
-
non-progressive mode
unsaturated disaccharide units
-
?
chondroitin 4-sulfate
?
show the reaction diagram
-
weak activity
-
-
?
chondroitin 6-sulfate
?
show the reaction diagram
-
weak activity
-
-
?
chondroitin sulfate
?
show the reaction diagram
-
-
-
-
ir
chondroitin sulfate
?
show the reaction diagram
-
-
-
-
?
chondroitin sulfate
?
show the reaction diagram
-
degradation
-
-
?
chondroitin sulfate
?
show the reaction diagram
Q53591
degradation
-
-
?
chondroitin sulfate
?
show the reaction diagram
Q53591
degrades progressively unsulfated and 6-sulfated regions from the reducing end
-
-
?
chondroitin sulfate
?
show the reaction diagram
-
non-progressive mode, no activity with chondroitin 4-sulfated at the nonreducing end, no activity with substrate sulfated at position 2
-
-
?
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)
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-PA
GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-PA
GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-GlcA-(1-3)GalNAc(4-sulfate)-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
show the reaction diagram
-
-
-
-
?
GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
GlcA-(1-3)GalNAc + GlcA-(1-3)GalNAc-(1-4)GlcA-(1-3)GalNAc-PA
show the reaction diagram
-
-
-
-
?
GlcA-GlcNAc-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA + H2O
GlcA-GlcNAc + GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
show the reaction diagram
-
-
-
-
?
hyaluronan
?
show the reaction diagram
-
-
-
-
?
hyaluronan
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
native enzyme and isolated N-terminal domain
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
Q53591
-
unsaturated disaccharide
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
unsaturated disaccharide units
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
disaccharide unit
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
from umbilical cord
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
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
show the reaction diagram
Q53591
elimination of the polymer in the host connective tissue
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q53591
progressive degradation from the reducing end
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
progressive mode of action, degradation
unsaturated disaccharide unit
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
progressive mode, preferred substrate
unsaturated disaccharide units
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
substrate structure
disaccharide unit
-
ir
hyaluronan
2-acetamido-2-deoxy-3-(beta-D-gluco-4-enepyranosyluronic acid)-glucose
show the reaction diagram
-
-
-
-
?
hyaluronan
2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-glucose
show the reaction diagram
-
from human umbilical cord
-
-
?
hyaluronan
fully O-sulfated oligosaccharides
show the reaction diagram
Streptomyces hyalurolyticus
-
from Streptococcus zooepidemicus, sodium salt, large scale depolymerization
chain length of 4-20, detection and composition analysis
-
?
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
-
degradation
-
-
?
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
Q53591
degradation
-
-
?
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronan + H2O
N-acetyl-beta-D-glucosamine + D-glucuronate
show the reaction diagram
Streptomyces hyalurolyticus
-
from Streptococcus zooepidemicus, degradation
-
-
?
hyaluronan + H2O
oligosaccharides
show the reaction diagram
-
specific for, degradation
-
-
?
hyaluronan hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
progressive mode of action, degradation
unsaturated disaccharide unit
-
?
hyaluronan hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
the longest segment that binds entirely within the active site, a cleft between alpha- and beta-domain
unsaturated disaccharide units
-
?
hyaluronan tetrasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
unsaturated disaccharide units
-
?
hyaluronate
?
show the reaction diagram
-
efficient degradation of hyaluronate
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
Q54873
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
unsaturated disaccharide
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
unsaturated disaccharides are released from the end of the hyaluronan chains
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
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
show the reaction diagram
Streptococcus agalactiae 4755
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
Staphylococcus aureus 1801
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
Staphylococcus aureus M18
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
Staphylococcus aureus AEMC 1801
-
-
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
Streptococcus dysgalactiae subsp. equisimilis SHL-03
-
-
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
O86478
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
P26831
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
Q59634
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
Streptomyces hyalurolyticus
-
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
Q9WXL3
eliminative reaction, degradation
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
eliminative reaction, degradation
-
-
?
hyaluronate hexasaccharide
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
Q53591
-
unsaturated disaccharide
-
?
hyaluronic acid
?
show the reaction diagram
-
-
-
-
?
hyaluronic acid
?
show the reaction diagram
-
-
-
-
?
hyaluronic acid
?
show the reaction diagram
-
from pig skin
-
-
?
hyaluronic acid
?
show the reaction diagram
-
from rooster comb
-
-
?
hyaluronic acid
?
show the reaction diagram
C0M9W4
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
?
show the reaction diagram
Streptococcus agalactiae 4755
-
-, from rooster comb
-
-
?
hyaluronic acid
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
hyaluronic acid
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
Streptomyces hyalurolytics
-
from pig skin
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
-
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Q53591
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
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
show the reaction diagram
Streptomyces hyalurolyticus
-
highly specific for hyaluronan, degradation, unsaturated products of varied size
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Q8VLQ8
the enzyme is essential for growth on hyaluronate as carbon source
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Streptomyces hyalurolyticus
-
highly specific for hyaluronan
primarily disaccharides, but also tetrasaccharides and hexasaccharides
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Q8VLQ8
native and recombinant serotype 7 enzyme, human umbelical cord hyaluronate
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Staphylococcus aureus 8325-4
-
degradation, degradation of hyaluronate in connective tissue of hosts to facilitate invasion by subcutaneous infection, the enzyme is an essential bacterial virulence factor
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
show the reaction diagram
-
degradation
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
show the reaction diagram
-
depolymerization
product identification by CE-MS, gel filtration, and viscosimetry
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
show the reaction diagram
Streptococcus agalactiae 4755
-
degradation
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
show the reaction diagram
Streptococcus agalactiae 4755
-
depolymerization
product identification by CE-MS, gel filtration, and viscosimetry
-
?
hyaluronic acid polymer
hyaluronic acid tetrasaccharide + hyaluronic acid hexasaccharide
show the reaction diagram
Streptomyces hyalurolyticus
-
hyaluronic acid purified from Mytilus galloprovincialis
-
-
?
iduronic acid-GalNAc-(1-4)GlcA-(1-3)GalNAc(4,6-disulfate)-GlcA-(1-3)GalNAc(4,6-disulfate)-GlcA-(1-3)GalNAc(4,6-disulfate)-PA
iduronic acid-GalNAc + GlcA-(1-3)GalNAc(4,6-disulfate)-GlcA-(1-3)GalNAc(4,6-disulfate)-GlcA-(1-3)GalNA(4,6-disulfate)-PA
show the reaction diagram
-
-
-
-
?
tetrasaccharides with a 6-sulfated disaccharide at the reducing end
?
show the reaction diagram
-
-
-
-
?
unsulfated chondroitin
?
show the reaction diagram
-
degradation
-
-
?
unsulfated chondroitin
?
show the reaction diagram
Q53591
degradation
-
-
?
iduronic acid-GalNAc-(1-4)GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
iduronic acid-GalNAc + GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-GlcA-(1-3)GalNAc(6-sulfate)-PA
show the reaction diagram
-
lower activity
-
-
?
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificty
-
-
-
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
?
-
O86478
phylogenetic analysis
-
-
-
additional information
?
-
-
phylogenetic analysis
-
-
-
additional information
?
-
Q59634
phylogenetic analysis
-
-
-
additional information
?
-
Streptomyces hyalurolyticus
-
phylogenetic analysis
-
-
-
additional information
?
-
Q9WXL3
phylogenetic analysis
-
-
-
additional information
?
-
-
phylogenetic analysis
-
-
-
additional information
?
-
Q53591
enzyme is a virulence factor that helps the pathogen to brake through the biophysical barrier of the host tissues
-
-
-
additional information
?
-
-
phylogenetic analysis, anti-phagocytic factors, such as M-protein, might provide sufficient protection for Streptococcus pyogenes infection during enzyme production
-
-
-
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
?
-
-
phylogenetic analysis, enzyme causes mastitis, may have an important role in promoting dissemination of the producing organism into host tissue
-
-
-
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
?
-
P26831
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
?
-
Clostridium difficile
-
phylogenetic analysis, enzyme may play a role in releasing nutrients thereby promoting establishment of the organism in the gut
-
-
-
additional information
?
-
-
phylogenetic analysis, strong association between the production of purulent abscesses and enzyme during infections
-
-
-
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
?
-
-
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
?
-
-
global regulators sar and agr are involved in enzyme regulation
-
-
-
additional information
?
-
Q6H8W8, Q6H8W9, Q6H8X0, Q6H8X1, Q6H8X2, Q6H8X4, Q6H8X5, Q6H8X6, Q6H8X7, Q6H8X8, Q6H8Y0, Q6H8Y1, Q6H8Y2, Q6H8Y3, Q6H8Y4, Q8VLQ7, Q8VLQ8, -
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 degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview
-
-
-
additional information
?
-
Q8VLQ8
the enzyme is involved in development of meningitis in infected pigs
-
-
-
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
?
-
Staphylococcus aureus 8325-4
-
global regulators sar and agr are involved in enzyme regulation
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hyaluronan
?
show the reaction diagram
-
-
-
-
?
hyaluronan
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
-
disaccharide unit
-
ir
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
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
show the reaction diagram
Q53591
elimination of the polymer in the host connective tissue
-
-
?
hyaluronan
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
-
enzyme might be involved in the pathogenicity of the bacterium causing paracocidiodomycosis
-
-
?
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronan
hyaluronic acid oligomers
show the reaction diagram
-
absolute substrate specificity of the bacteriophage enzyme
-
-
?
hyaluronate
?
show the reaction diagram
-
efficient degradation of hyaluronate
-
-
?
hyaluronic acid
?
show the reaction diagram
-
-
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Q53591
degradation of hyaluronate in connective tissue of hosts to facilitate invasion
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
-
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
show the reaction diagram
Streptomyces hyalurolyticus
-
highly specific for hyaluronan, degradation, unsaturated products of varied size
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Q8VLQ8
the enzyme is essential for growth on hyaluronate as carbon source
-
-
?
hyaluronic acid
?
show the reaction diagram
Streptococcus agalactiae 4755
-
-
-
-
?
hyaluronic acid
hyaluronic acid oligomers
show the reaction diagram
Staphylococcus aureus 8325-4
-
degradation of hyaluronate in connective tissue of hosts to facilitate invasion by subcutaneous infection, the enzyme is an essential bacterial virulence factor
-
-
?
hyaluronic acid polymer
hyaluronic acid oligomers
show the reaction diagram
Streptococcus agalactiae, Streptococcus agalactiae 4755
-
degradation
-
-
?
additional information
?
-
O86478
phylogenetic analysis
-
-
-
additional information
?
-
-
phylogenetic analysis
-
-
-
additional information
?
-
Q59634
phylogenetic analysis
-
-
-
additional information
?
-
Streptomyces hyalurolyticus
-
phylogenetic analysis
-
-
-
additional information
?
-
Q9WXL3
phylogenetic analysis
-
-
-
additional information
?
-
-
phylogenetic analysis
-
-
-
additional information
?
-
Q53591
enzyme is a virulence factor that helps the pathogen to brake through the biophysical barrier of the host tissues
-
-
-
additional information
?
-
-
phylogenetic analysis, anti-phagocytic factors, such as M-protein, might provide sufficient protection for Streptococcus pyogenes infection during enzyme production
-
-
-
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
?
-
-
phylogenetic analysis, enzyme causes mastitis, may have an important role in promoting dissemination of the producing organism into host tissue
-
-
-
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
?
-
P26831
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
?
-
Clostridium difficile
-
phylogenetic analysis, enzyme may play a role in releasing nutrients thereby promoting establishment of the organism in the gut
-
-
-
additional information
?
-
-
phylogenetic analysis, strong association between the production of purulent abscesses and enzyme during infections
-
-
-
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
?
-
-
global regulators sar and agr are involved in enzyme regulation
-
-
-
additional information
?
-
Q6H8W8, Q6H8W9, Q6H8X0, Q6H8X1, Q6H8X2, Q6H8X4, Q6H8X5, Q6H8X6, Q6H8X7, Q6H8X8, Q6H8Y0, Q6H8Y1, Q6H8Y2, Q6H8Y3, Q6H8Y4, Q8VLQ7, Q8VLQ8, -
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 degradation of hyaluronate from connective host tissues to facilitate the host and specific tissue invasion by the bacterium, overview
-
-
-
additional information
?
-
Q8VLQ8
the enzyme is involved in development of meningitis in infected pigs
-
-
-
additional information
?
-
Staphylococcus aureus 8325-4
-
global regulators sar and agr are involved in enzyme regulation
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
binding modulates enzyme structure
Ca2+
-
activates, bridges between enzyme and substrate
Ca2+
-
activates
NaCl
Streptomyces hyalurolyticus
-
-
additional information
-
calcium ions do not interact with the enzyme, and its role actually is in modulating the hyaluronan conformation and not in the functional regulation of enzyme
additional information
C0M9W4
no requirement for any specific divalent ion tested
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(13Z)-docos-13-enoic acid
-
strong inhibition
(13Z)-docos-13-enoic acid
Streptomyces hyalurolytics
-
weak inhibition
(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
Q53591
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
1,3-benzoxazole-2(3H)-thione
-
-
1,3-diacetyl-1H-benzo[d]imidazol-2(3H)-one
-
10% inhibition
1,3-diacetyl-benzimidazole-2-thione
Q53591
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
Q53591
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-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
-
-
arachidic acid
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
weak inhibition
behenic acid
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
weak inhibition
benzyl 2-thioxobenzo[d]oxazol-3(2H)-carboxylate
-
-
beta1,4-galacto-oligosaccharides
-
partially sulfated and non-sulfated forms, IC50 values
-
Ca2+
-
slight inhibition by 30% unfolding of the enzyme by ion binding
capric acid
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
weak inhibition
D-isoascorbic acid
Streptomyces hyalurolyticus
-
strong inhibition
D-saccharic-1,4-lactone
Streptomyces hyalurolyticus
-
strong inhibition
dehydroascorbic acid
Streptomyces hyalurolyticus
-
-
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
Streptomyces hyalurolytics
-
weak inhibition
guanidine hydrochloride
-
strong inhibition, unfolding within 1 h
guanidine isothiocyanate
-
strong inhibition
iodoacetate
-
10 mM, complete inhibition
L-arginine
-
strong inhibition
L-arginine methyl ester
-
strong inhibition
L-ascorbic acid
Streptomyces hyalurolyticus
-
strong inhibition
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
lanostanoid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.051 mM
lauric acid
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
weak inhibition
linoleic acid
Streptomyces hyalurolytics
-
weak inhibition
linolenic acid
Streptomyces hyalurolytics
-
weak inhibition
methyl (9Z)-octadecenoate
-
-
methyl (9Z)-octadecenoate
Streptomyces hyalurolytics
-
weak inhibition
methyl 2-sulfanylbenzo[d]oxazole-5-carboxylate
-
27% inhibition
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
-
-
myristic acid
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
weak inhibition
myristoleic acid
Streptomyces hyalurolytics
-
weak inhibition
N-(3-phenylpropionyl)-benzoxazole-2-thione
-
-
N-(3-phenylpropionyl)benzoxazole-2-thione
-
-
NaCl
-
slight inhibition, wild-type and mutant enzymes
nervonic acid
-
strong inhibition
nervonic acid
Streptomyces hyalurolytics
-
weak inhibition
oleic acid
Streptomyces hyalurolytics
-
weak inhibition
palmitic acid
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
weak inhibition
palmitoleic acid
Streptomyces hyalurolytics
-
weak 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
-
petroselinic acid
-
strong inhibition
petroselinic acid
Streptomyces hyalurolytics
-
weak inhibition
polyporenic acid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0125 mM
ricinoleic acid
Streptomyces hyalurolytics
-
weak inhibition
saccharic acid
Streptomyces hyalurolyticus
-
-
stearic acid
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
weak inhibition
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
vaccenic acid
-
strong inhibition
vaccenic acid
Streptomyces hyalurolytics
-
weak inhibition
Mg2+
-
slight inhibition by 30% unfolding of the enzyme by ion binding
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
-
additional information
-
no inhibition and conformational change induced by NaCl
-
additional information
-
inhibition curves, overview
-
additional information
Q53591
structure-based design of bacterial hyaluronan lyase inhibitors, combinatorial chemistry database and crystal structure, method, overview
-
additional information
-
IC50 for 1,3-diacetylbenzimidazole-2-thione is above 0.1 mM
-
additional information
C0M9W4
not inhibited by ascorbic acid at concentration up to 20 mM
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CD44
Q12794, Q12891
intracellular hyaluronic acid degradation is predominantly mediated by Hyal-1 after incorporation of hyaluronic acid by CD44; without CD44 expression, Hyal-2 exists in a granular pattern, and does not show hyaluronidase activity
-
additional information
-
enzyme is induced by the presence of substrate
-
additional information
-
the enzyme is synthesized as inactive zymogen in the cell and then secreted and activated by cleavage of the signal peptide
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.05
-
hyaluronan
-
recombinant mutant N349A, pH 6.0, 22C
-
0.08
-
hyaluronan
-
mutant F343V, pH 6.0, 37C
-
0.09
-
hyaluronan
-
wild-type enzyme, pH 6.0, 37C
-
0.12
-
hyaluronan
-
recombinant wild-type enzyme and mutant Y408F, pH 6.0, 22C
-
0.17
-
hyaluronan
-
recombinant mutantR243V, pH 6.0, 22C
-
0.6
-
hyaluronan
-
mutant W292A, pH 6.0, 37C
-
0.99
-
hyaluronan
-
recombinant mutants H399A and N580A, pH 6.0, 22C
-
3.8
-
hyaluronan
-
mutant W292A/F343V, pH 6.0, 37C
-
0.08
-
hyaluronan hexasaccharide
-
recombinant wild-type enzyme, pH 6.0, 22C
0.38
-
hyaluronate
-
-
0.44
-
hyaluronate
-
pH 5.5, 37C, recombinant enzyme
0.71
-
hyaluronic acid
C0M9W4
concentration expressed as the concentration of its disaccharide unit (equivalent to 0.29 mg/ml)
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic mechanism, kinetics, pH 6.0, 22C
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetic mechanism
-
additional information
-
additional information
-
Km-values of 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)
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
chondroitin sulfate
-
after 14 h at pH 5.0 (fibrillar film formation) 20% activity (100% activity at pH 7.0, 0 h, with hyaluronic acid)
4.9
-
hyaluronan
-
recombinant enzyme, pH 6.0, 30C
-
additional information
-
hyaluronic acid
-
after 15 h at pH 5.0 (fibrillar film formation) 68% activity (100% activity at pH 7.0, 0 h, with hyaluronic acid)
7.61
-
hyaluronic acid
C0M9W4
-
additional information
-
additional information
-
turnover numbers of 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)
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0035
-
(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
0.16
0.31
(2E)-1-furan-2-yl-3-(4-nitrophenyl)prop-2-en-1-one
Q53591
IC50 at enzyme optimum pH 5.0 is 0.31 mM, and 0.16 mM at physiological pH 7.4
0.07
-
(3-chlorophenyl)(2-thioxo-1H-benzo[d]imidazol-1-yl)methanone
-
pH 7.4, 37C
2.54
-
1,3-benzoxazole-2(3H)-thione
-
pH 7.4, 37C
0.0001
-
1,3-diacetyl-1H-benzo[d]imidazol-2(3H)-one
-
pH 7.4, temperature not specified in the publication
0.005
0.16
1,3-diacetyl-benzimidazole-2-thione
Q53591
IC50 at enzyme optimum pH 5.0 is 0.16 mM, and 0.005 mM at physiological pH 7.4
0.005
-
1,3-diacetylbenzimidazole-2-thione
-
pH 7.4, temperature not specified in the publication
1.86
-
1,3-dihydro-2H-benzimidazole-2-thione
-
pH 7.4, 37C
0.029
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)-3-phenylpropan-1-one
-
pH 7.4, 37C
0.02
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)butan-1-one
-
pH 7.4, 37C
-
0.017
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)ethanone
-
pH 7.4, 37C
0.016
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)hexan-1-one
-
pH 7.4, 37C
0.026
-
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)propan-1one
-
pH 7.4, 37C
0.025
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)decan-1-one
-
pH 7.4, 37C
0.042
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
pH 7.4, 37C
0.017
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexadecan-1-one
-
pH 7.4, 37C
0.029
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)hexan-1-one
-
pH 7.4, 37C
0.048
-
1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
pH 7.4, 37C
0.012
-
1-(3-acetyl-1,2-dihydro-2-thioxobenzo[d]imidazol-1-yl)hexan-1-one
-
pH 7.4, temperature not specified in the publication
0.019
-
1-(3-ethyl-1,2-dihydro-2-thioxobenzo[d]imidazole-1-yl)ethanone
-
pH 7.4, temperature not specified in the publication
0.011
-
1-decyl-2-(4-sulfamoyloxyphenyl)-1-indol-6-yl sulfamate
-
pH 5.0
0.9
0.37
2,2'-benzene-1,4-diyldiacetic acid
Q53591
IC50 at enzyme optimum pH 5.0 is 0.37 mM, and 0.90 mM at physiological pH 7.4
0.062
-
2-phenoxy-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
pH 7.4, 37C
0.069
-
2-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone
-
pH 7.4, 37C
1.45
-
3-acetylbenzo[d]oxazol-2(3H)-one
-
pH 7.4, 37C
0.02
-
3-cyclohexyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
pH 7.4, 37C
0.024
-
3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
-
pH 7.4, 37C
0.04
-
3alpha-acetylpolyporenic acid A
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.040 mM
0.019
-
4-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)butan-1-one
-
pH 7.4, 37C
0.556
-
benzyl 2-thioxobenzo[d]oxazol-3(2H)-carboxylate
-
pH 7.4, 37C
6.1
-
L-ascorbic acid
-
pH 5.0
34.8
-
L-ascorbic acid
-
pH 5.0
0.0042
-
L-ascorbic acid-6-hexadecanoate
-
pH 5.0
0.1
-
L-ascorbic acid-6-hexadecanoate
-
pH 5.0
0.051
-
lanostanoid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.051 mM
0.021
-
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
-
pH 7.4, 37C
0.015
-
N-(3-phenylpropionyl)-benzoxazole-2-thione
-
pH 5.0
0.015
-
N-(3-phenylpropionyl)benzoxazole-2-thione
-
pH 5.0, 37C
0.024
-
N-(3-phenylpropionyl)benzoxazole-2-thione
-
pH 7.4, 37C
0.015
-
partially sulfated planteose
-
the non-sulfated planteose is not inhibitory, IC50 is 0.015 mM
0.03
-
partially sulfated verbascose
-
2 forms, the non-sulfated verbascose is not inhibitory, IC50 are 0.030 mM and 0.001 mM
-
0.0125
-
polyporenic acid
-
from Piptoporus betulinus inhibiting bacterial hyaluronate lyase, structure determination by NMR, IC50 is 0.0125 mM
0.35
-
sulfated 2-hydroxyphenyl monolactobioside
-
IC50 is 0.35 mM
-
0.08
-
sulfated hydroquinone galactoside
-
IC50 is 0.080 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.19
-
-
mutant W292A/F343V, in absence of NaCl
4.3
-
-
mutant W292A, in absence of NaCl
9.62
-
-
pH 5.5, 37C, purified recombinant enzyme
68.9
-
-
mutant F343V, in absence of NaCl
231.4
-
-
wild-type enzyme, in absence of NaCl
3571
-
-
purified 92 kDa mature form
3680
-
-
purified 111 kDa pro-form
400000
-
O86478
stabilized by addition of 5 mg ovalbumin/mg hyaluronate lyase
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity in pharmaceutical preparations
additional information
-
-
-
additional information
-
-
activity in different isolated strains from several sources, overview
additional information
-
-
activity of wild-type and mutant enzymes in diameter of clear zone produced on HA plates in centimeters
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
7.4
-
assay at
5.5
-
Q8VLQ8
assay at
6
7
Q12794, Q12891
Hyal-2
6
-
-
and a second optimum at pH 8.6
6
-
Streptomyces hyalurolyticus
-
assay at
6
-
Streptomyces hyalurolyticus
-
assay at
6.2
-
Streptococcus dysgalactiae, Streptomyces hyalurolytics
-
phosphate buffer, assay at
6.5
-
Streptomyces hyalurolyticus
-
assay at
6.8
-
-
assay at
8.6
-
-
and a second optimum at pH 6.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
7
-
high activity at pH 3.0-4.0, lower activity at pH 7.0
3
8
-
activity range, profile overview
4.6
7
-
pH 4.6: about 75% of maximal activity, pH 7.0: about 45% of maximal activity
5
8
-
pH 5.0: about 60% of maximal activity, pH 8.0: about 45% of maximal activity
5
9
-
pH 5.0: about 40% of maximal activity, pH 9.0: about 55% of maximal activity
5.5
7.5
Q12794, Q12891
pH 5.5: about 55% of maximal activity, pH 7.5: about 40% of maximal activity
6
6.8
-
pH 6.0: optimum, pH 6.8: 40% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
Streptomyces hyalurolyticus
-
assay at room temperature
37
-
Streptomyces hyalurolyticus
-
assay at
37
-
Q6H8W8, Q6H8W9, Q6H8X0, Q6H8X1, Q6H8X2, Q6H8X4, Q6H8X5, Q6H8X6, Q6H8X7, Q6H8X8, Q6H8Y0, Q6H8Y1, Q6H8Y2, Q6H8Y3, Q6H8Y4, Q8VLQ7, Q8VLQ8
assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at
37
-
Q8VLQ8
assay at
37
-
C0M9W4
50% activity at 44C
60
-
Streptomyces hyalurolytics
-
assay at
60
-
Streptomyces hyalurolyticus
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
activity range, profile overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
4.7
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Streptomyces hyalurolyticus
-
-
Manually annotated by BRENDA team
Streptococcus agalactiae 4755
-
purified enzyme
-
Manually annotated by BRENDA team
-
acidic, somatic hyaluronidase 3 exists in two isoforms, and resides on the plasma membrane over the head and midpiece
Manually annotated by BRENDA team
-
caput, corpus, and caudal mouse sperm. Acidic, somatic hyaluronidase 3 exists in two isoforms, and resides on the plasma membrane over the head and midpiece
Manually annotated by BRENDA team
-
HYAL3, which belongs to the somatic subgroup of hyases, is abundantly expressed in the testis
Manually annotated by BRENDA team
-
Hyal3 and SPAM1
Manually annotated by BRENDA team
additional information
-
wild-type enzyme expression is maximal during mid-exponential growth phase
Manually annotated by BRENDA team
additional information
-
Hyal3 tissue expreesion pattern, overview
Manually annotated by BRENDA team
additional information
-
Hyal3 tissue expreesionpattern, overview
Manually annotated by BRENDA team
additional information
Staphylococcus aureus 8325-4
-
wild-type enzyme expression is maximal during mid-exponential growth phase
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is anchored via its carboxy-terminal part to the pneumococcal cell wall by a covalent linkage with peptidoglycan structures
Manually annotated by BRENDA team
-
enzyme is relaesed only when the pneumolysin causes lysis of the pneumococci
Manually annotated by BRENDA team
-
enzyme is relaesed only when the pneumolysin causes lysis of the pneumococci
-
Manually annotated by BRENDA team
Staphylococcus aureus M18
-
-
-
-
Manually annotated by BRENDA team
Q12794, Q12891
Hyal-2 activityis detected in the membrane fraction of cells co-expressing Hyal-2 and CD44
Manually annotated by BRENDA team
additional information
Q12794, Q12891
although Hyal-1 is active only in intracellular space in vivo, a certain amount of the enzyme is secreted to extracellular space. This extracellular Hyal-1 is incorporated by cells and such uptake of Hyal-1 is, in part, involved in the intracellular degradation of hyaluronic acid
-
Manually annotated by BRENDA team
additional information
-
differential localization of sperm isozymes, pH-dependent, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Streptococcus agalactiae serotype III (strain NEM316)
Streptococcus agalactiae serotype III (strain NEM316)
Streptococcus agalactiae serotype III (strain NEM316)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70000
75000
-
gel filtration
70000
-
-
gel filtration
83280
-
-
mass spectrometry experiments
84000
-
-
isoenzyme C, gel filtration
84000
-
-
gel filtration
85110
-
-
gel filtration
91000
107000
-
the recombinantly expressed enzyme exists in different proteolytically fragmented forms of the full-length enzyme with Mr of 107 kDa
92000
-
-
autocatalytically processed enzyme, gel filtration
92000
-
-
gel filtration
110000
-
-
recombinant enzyme, gel filtration
110000
-
-
gel filtration
111000
-
-
pro-form, gel filtration
126500
130000
Q8VLQ8
amino acid sequence calculation and native PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 126000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x 82000, calculation from nucleotide sequence
?
-
x * 100000, SDS-PAGE, x * 85000, SDS-PAGE, x * 75000-50000, trypsin digested enzyme, SDS-PAGE
?
P26831
x * 114000, amino acid sequence calculation
?
Q59634
x * 82000, amino acid sequence calculation
?
-
x * 92000, amino acid sequence calculation
?
O86478
x * 121000, amino acid sequence calculation
?
-
x * 107000, amino acid sequence calculation
?
Q53591
3 different form of 118, 111, and 92 kDa, the 118 kDa form is inactive
?
Q53591
x * 92000, SDS-PAGE
?
-
x * 41000, N-terminal domain, SDS-PAGE, x * 41000, C-terminal domain, SDS-PAGE
?
-
x * 83208, mutant W292A, mass spectrometry, x * 83273, mutant F343V, mass spectrometry, x * 83097, mutant W291A/W292A, mass spectrometry, x * 83102, mutant W292A/F343V, mass spectrometry, x * 83027, mutant W291A/W292A/F343V, mass spectrometry
?
Q8VLQ8
x * 54260, sequence calculation
?
C0M9W4
x * 42000, SDS-PAGE
?
-
x * 40000, about, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 47000 + x * 55000, HYAL3 in sperm, SDS-PAGE
?
-
x * 44000 + x * 47000, HYAL3 in sperm, SDS-PAGE
homotrimer
-
pH 7.0, aggregation at pH 5.0, gel filtration, SDS-PAGE after chemical cross-linking
trimer
-
3 * 36000-36900, SDS-PAGE and ESI-MS
monomer
-
1 * 80000, SDS-PAGE; x * 83218, calculation from nucleotide sequence
additional information
-
N-terminal alpha- and C-terminal beta-domain structure determination, determination of interface residues, overview
additional information
Q53591
enzyme is composed of 2 domains, alpha-helical alpha-domain and beta-sheet beta-domain, which are structurally and functionally distinct
additional information
-
enzyme consists of 2 structural domains, C-terminal and N-terminal, each of which folds and unfolds independent from the other due to lack of cooperative interactions between them, structure determination
additional information
-
homology model from crystal structure
additional information
-
the enzyme contains a distorted (alpha/alpha)5-6 barrel composed of alpha-helices inside and out, substrate binding is facilitated by the predominantly positive and hydrophobic cleft located at the top of the wider end of the barrel nested among helices and interhelix loops, domain structure, overview
additional information
-
the enzyme is very short in sequence and different in structure compared to enzymes of other species
additional information
Streptomyces hyalurolyticus
-
domain structure, overview
additional information
-
the three-dimensional enzyme structure contains a catalytic alpha-domain at the N-terminus and a C-terminal supportive cell-wall-anchoring beta-domain connected by a short peptide linker
additional information
-
three-dimensional structure analysis, unfolding process using 1-4 M guanidinium hydrochloride, effects of unfolding on the structure, transitions, kinetics, overview
additional information
-
three-dimensional structure analysis, active site structure and hydrophobic patch, structure-function relationship
additional information
-
structure analysis, active site structure and hydrophobic patch, structure-function relationship
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
contains neutral sugars galactose, glucose, and mannose in the ratio 1:3:6. Amino sugars galactosamine and glucosamine, or mannosamine are present in the ratio 1:1
side-chain modification
-
-
side-chain modification
Staphylococcus aureus 1801
-
-
-
proteolytic modification
-
autocatalytic conversion to a smaller 92kDa active enzyme form, completely prevented by 2 mM EDTA
proteolytic modification
Q53591
activation probably by autolytic cleavage
proteolytic modification
-
the enzyme is synthesized as inactive zymogen in the cell and then secreted and activated by cleavage of the signal peptide
proteolytic modification
-
the enzyme is synthesized as inactive zymogen int he cell and then secreted and activated by cleavage of the signal peptide
side-chain modification
-
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q53591
purified free enzyme and enzyme-product complex, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
Q53591
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, 22C, 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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
-
-
18 h, complete loss of activity
2
13
-
18 h, stable
4
7
-
purified recombinant enzyme, stable
4.2
-
-
37C, 1 h, 80% loss of activity
5
5.8
-
37C, 1 h, stable
5.5
-
-
30 min, irreversible inactivation
7
-
-
37C, 1 h, 70% loss of activity
7
-
-
above pH 7.0, 24 h, irreversible loss of activity
8.6
-
-
10 min, complete loss of activity
14
-
-
18 h, complete loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
24 h, 40% loss of activity
20
-
-
room temperature, 3 h, 50% loss of activity
20
-
-
room temperaure, stable
20
-
-
room temperature, pH 7.2, 15 h, stable
25
45
-
purified recombinant enzyme, stable
37
-
-
1 h, stable; stable
45
-
-
1 h, inactivation
50
-
-
pH 5.8, 15 min, complete inactivation
55
-
-
partially unfolding
56
-
-
unstable at
56
-
-
20 min, almost complete loss
additional information
-
-
-
additional information
-
-
transition temperatures
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable through 5 cycles of freezing and thawing
-
in repeated batch culture, stable during 158.5-245.0 h and probably longer
-
the C-terminal domain is less stable against thermal and guanidine hydrochloride denaturation than the N-terminal domain
-
reducing agents required to stabilize the purified enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
no significant difference between aerobic and anaerobic denaturation constants
-
210750
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for 1 year
-
frozen 25% loss of activity after 1 week
-
-20C, stable for 2 years
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial, isoenzyme A, B and C
-
cloning overexpression, and purification of SagHL and its different fragments/domains
-
recombinant enzyme
-
recombinant enzyme from Escherichia coli
Q53591
recombinant wild-type and mutant enzymes from Escherichia coli
-
cloning, overexpression and purification of the 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)
-
isolated N-terminal domain from purified recombinant native enzyme
-
recombinant enzyme
-
recombinant wild-type and mutant enzymes from Escherichia coli
-
type 24, strain G54
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) to homogeneity by ion exchange and nickel affinity chromatography, and gel filtration
-
partially, recombinant enzyme from Escherichia coli
-
recombinant His-tagged enzyme 53.4fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and cation exchange chromatography
-
native enzyme from serotype 7 to over 95% purity, recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
Q8VLQ8
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
293 cells stably express Hyal-2; Hyal-1/293 and Hyal-1/CD44/293 are stably overexpressing Hyal-1. The expressed Hyal-1 is not only accumulated intracellularly, but is also secreted to the outside of the cells
Q12794, Q12891
expression in Escherichia coli
-
complementation of an enzyme-deficient mutant strain by expression of hysA
-
cloning overexpression, and purification of SagHL and its different fragments/domains
-
DNA sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli
-
expression in Escherichia coli
-
overexpression of the enzymes from strains 3502 and 4755 in Escherichia coli
Q53591
His-tagged version expressed in Escherichia coli BL21(DE3)
C0M9W4
cloning, overexpression and purification of the C-terminal domain swapped chimeras of SpnHL and SagHL (hyaluronate lyase from Streptococcus agalactiae), modified enzyme SpnHLv/SagHLv (where the size of linker connecting the alpha-domain to C-terminal domain is enlarged by two amino acid)
-
expression in Escherichia coli resulting in different protein sizes
-
overexpression of fully functional truncated wild-type and mutant enzymes in Escherichia coli
-
overexpression of His-tagged enzyme in Escherichia coli
-
overexpression of mutant Y408F in Escherichia coli
-
overexpression of wild-type and mutant enzymes in Escherichia coli
-
overexpression of wild-type and mutant enzymes in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10
A7XFU3, A7XFU4, A7XFV0, A7XFV1, Q9L7W9
overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli BL21(DE3)
-
recombinant expression of the C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)/pET30b-hylp
-
expressed in Escherichia coli TOP10
Q99ZX4
expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10
A7XFU7, A7XFU8, A7XFU9, A7XFV3, A7XFV4, A7XFV6, A7XFV7
expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10; expressed in Escherichia coli TOP10
A7XFU5, A7XFU6, A7XFV2, A7XFV5
expressed in Escherichia coli TOP10
-
gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview; gene hyl, distribution, genetic diversity, and variable expression within the Streptococcus suis population, 309 isolates of different serotypes, geographic sources, and clinical backgrounds, overview
Q6H8W8, Q6H8W9, Q6H8X0, Q6H8X1, Q6H8X2, Q6H8X4, Q6H8X5, Q6H8X6, Q6H8X7, Q6H8X8, Q6H8Y0, Q6H8Y1, Q6H8Y2, Q6H8Y3, Q6H8Y4, Q8VLQ7, Q8VLQ8
gene hyl, DNA and amino acid sequence determination and analysis, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q8VLQ8
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
C0M9W4
catalytic mutant, 8% activity
Y183A
C0M9W4
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
H399A
-
site-directed mutagenesis, highly reduced activity compared to wild-type enzyme
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
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
Y408F
-
site-directed mutagenesis, inactive mutant
Y408F
-
enzyme substrate complex structure determination by crystallization
Y408F
-
the mutant enzyme is inactive
D199V
A7XFU3, A7XFU4, A7XFV0, A7XFV1, Q9L7W9
loss of activity
V199D
Q99ZX4
gain of enzymatic activity from a previously inactive protein, numbering based on the sequence of HylA from strain 10403 (M-22)
V199D
Streptococcus pyogenes serotype M1 SF370
-
gain of enzymatic activity from a previously inactive protein, numbering based on the sequence of HylA from strain 10403 (M-22)
-
V199D
A7XFU7, A7XFU8, A7XFU9, A7XFV3, A7XFV4, A7XFV6, A7XFV7
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
Staphylococcus aureus 8325-4
-
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
-
M659G/D661K/K725L/T726W
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
additional information
-
mutation of the catalytic residues Asn429, His479, and Tyr488 inactivates the enzyme
H399A
-
the mutant enzyme shows 12% of wild-type enzyme activity
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)
V199D
Streptococcus pyogenes serotype M3 1055
-
mutant and wild-type protein have no enzymatic activity, numbering based on the sequence of HylA from strain 10403 (M-22)
-
additional information
Q8VLQ8
construction of an enzyme deficient strain by allelic relacement knockout of serotype 7
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
transient perfusion induces acute hypoxia and may limit the radiotherapy response and induce drug resistance. Hyaluronidase improves perfusion in human osteosarcoma xenografts grown orthotopically and in dorsal skinfold chambers
medicine
-
safe and effective in an intracytoplasmic sperm injection treatement program
medicine
-
as compared to bovine-derived enzyme cumulase is safe and effective in an intracytoplasmic sperm injection treatement program and can provide comparable if not improved parameters, including fertilization and embryo developmental rates
medicine
-
antitumor activity and overall survival of mice bearing highly aggessive tumors are significantly improved by codelivery of oncolytic adenovirus and hyaluronidase when compared with either of the monotherapy-treated groups, and it may prove to be a potent and novel approach to treating patients with cancer
pharmacology
-
enzyme can be used for production of pharmaceuticals as an alternative to bovine testicular hyaluronidase, BTH, because the production of BTH is stopped due to risk of BSE
pharmacology
Q53591
the enzyme is a target for structure-based design of selective inhibitors as drugs in bacterial infection therapy
pharmacology
O86478
in vitro microbial hyaluronate lyase is able to split the hyaluronic acid in atherosclerotic plaques under release of calcium deposits and reduces in vivo the development of atherosclerotic lesions in hyperlipidaemic rabbits
medicine
-
the enzyme can be used as a vaccine
pharmacology
-
enzyme is a target for inhibitor design
pharmacology
-
enzyme is a target for development of antimicrobial agents
pharmacology
-
the enzyme is a target for structure-based design of selective inhibitors as drugs in bacterial infection therapy
analysis
-
application for the specific determination of hyaluronan concentration
synthesis
Streptomyces hyalurolyticus
-
enzymatic production of fully O-sulfated oligosaccharides by large scale depolymerization of hyaluronan polymer