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Literature summary extracted from

  • Stern, R.; Jedrzejas, M.J.
    Hyaluronidases: their genomics, structures, and mechanisms of action (2006), Chem. Rev., 106, 818-839.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.35 isozymes are clustered on chromosome 9F1-F2 and 6A2, expression profiles Mus musculus
3.2.1.35 isozymes Hyal1-Hyal4, sequence comparison, the genes encoding isozymes Hyal1-Hyal3 are tightly clustered on chromosome 3q21.3, Hyal4 and HPH-20 are clustered on 7q31.3, expression profiles Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.35 three-dimensional structure analysis Bos taurus
3.2.1.35 three-dimensional structure analysis Apis mellifera
4.2.2.1 crystal structure analysis Streptococcus pneumoniae

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.35 D146N site-directed mutagenesis of HPH-20, the mutant shows highly reduced activity Homo sapiens
3.2.1.35 E148Q site-directed mutagenesis of HPH-20, inactive mutant Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.35 acrosome spermatid, HPH-20 Homo sapiens
-
-
3.2.1.35 extracellular venom Apis mellifera
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.35 hyaluronan + H2O Mus musculus
-
 hyaluronan oligomers
-
 ?
3.2.1.35 hyaluronan + H2O Bos taurus
-
 hyaluronan oligomers
-
 ?
3.2.1.35 hyaluronan + H2O Apis mellifera
-
 hyaluronan oligomers
-
 ?
3.2.1.35 hyaluronan + H2O Homo sapiens the enzyme is required for fertility facilitating the penetration of sperm through the cumulus mass in the ovum hyaluronan oligomers
-
 ?
3.2.1.35 additional information Homo sapiens HPH-20 or SPAM1, sperm adhesion molecule 1, is a bifunctional enzyme, which is also an adhesion molecule with binding properties to the cumulus mass surrounding the ovum ?
-
 ?
4.2.2.1 hyaluronan Streptococcus pyogenes phage H4489A absolute substrate specificity of the bacteriophage enzyme hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid Streptococcus agalactiae degradation hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid Streptococcus pneumoniae degradation hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid Streptomyces hyalurolyticus highly specific for hyaluronan, degradation, unsaturated products of varied size hyaluronic acid oligomers
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.35 Apis mellifera Q08169
-
-
3.2.1.35 Bos taurus
-
-
-
3.2.1.35 Homo sapiens
-
 isozymes Hyal1-Hyal4, and HPH-20, or SPAM1
-
3.2.1.35 Mus musculus
-
-
-
4.2.2.1 Streptococcus agalactiae
-
-
-
4.2.2.1 Streptococcus pneumoniae Q54873
-
-
4.2.2.1 Streptococcus pyogenes phage H4489A
-
 gene hylP
-
4.2.2.1 Streptomyces hyalurolyticus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.35
-
 Bos taurus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.35 hyaluronic acid hexasaccharide + H2O = hyaluronic acid disaccharide + hyaluronic acid tetrasaccharide reaction mechanism and three-dimensional structure Mus musculus
a
3.2.1.35 hyaluronic acid hexasaccharide + H2O = hyaluronic acid disaccharide + hyaluronic acid tetrasaccharide reaction mechanism and three-dimensional structure, catalytic residue is Glu113, substrate positioning residues, overview Apis mellifera
a
3.2.1.35 hyaluronic acid hexasaccharide + H2O = hyaluronic acid disaccharide + hyaluronic acid tetrasaccharide reaction mechanism and three-dimensional structure, catalytic residue is Glu149, substrate positioning residues, overview Bos taurus
a
3.2.1.35 hyaluronic acid hexasaccharide + H2O = hyaluronic acid disaccharide + hyaluronic acid tetrasaccharide reaction mechanism and three-dimensional structure, catalytic residues of isozymes Hyal1-Hyal4 are Glu131, Glu135, Glu129, and Glu147, respectively, substrate positioning residues, active site structure of isozymes, overview Homo sapiens
a
4.2.2.1 [hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate binding of negatively charged hydrophobic substrates is facilitated by the predominantly positive and hydrophobic cleft located at distorted (alpha/alpha)5-6 barrel, mechanism of hyaluronan degradation, active site residues are Asn349, His399, and Tyr408, overview Streptococcus pneumoniae
a
4.2.2.1 [hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate binding of negatively charged hydrophobic substrates is facilitated by the predominantly positive and hydrophobic cleft located at distorted (alpha/alpha)5-6 barrel, mechanism of hyaluronan degradation, overview Streptococcus agalactiae
a
4.2.2.1 [hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate mechanism of hyaluronan degradation, random endolytic action pattern, overview Streptomyces hyalurolyticus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.35 breast HPH-20 Homo sapiens
-
3.2.1.35 commercial preparation testicular Bos taurus
-
3.2.1.35 epididymis HPH-20 Homo sapiens
-
3.2.1.35 ovary HPH-20 Homo sapiens
-
3.2.1.35 spermatid HPH-20 Homo sapiens
-
3.2.1.35 spermatozoon
-
 Homo sapiens
-
3.2.1.35 testis
-
 Bos taurus
-
3.2.1.35 testis HPH-20 Homo sapiens
-
3.2.1.35 uterus HPH-20 Homo sapiens
-
3.2.1.35 venom
-
 Apis mellifera
-
4.2.2.1 commercial preparation
-
 Streptomyces hyalurolyticus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.35 additional information
-
 commercial preparation Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.35 hyaluronan + H2O
-
 Mus musculus hyaluronan oligomers
-
 ?
3.2.1.35 hyaluronan + H2O
-
 Homo sapiens hyaluronan oligomers
-
 ?
3.2.1.35 hyaluronan + H2O
-
 Bos taurus hyaluronan oligomers
-
 ?
3.2.1.35 hyaluronan + H2O
-
 Apis mellifera hyaluronan oligomers
-
 ?
3.2.1.35 hyaluronan + H2O the enzyme is required for fertility facilitating the penetration of sperm through the cumulus mass in the ovum Homo sapiens hyaluronan oligomers
-
 ?
3.2.1.35 additional information HPH-20 or SPAM1, sperm adhesion molecule 1, is a bifunctional enzyme, which is also an adhesion molecule with binding properties to the cumulus mass surrounding the ovum Homo sapiens ?
-
 ?
4.2.2.1 hyaluronan absolute substrate specificity of the bacteriophage enzyme Streptococcus pyogenes phage H4489A hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid
-
 Streptococcus agalactiae hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid
-
 Streptococcus pneumoniae hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid degradation Streptococcus agalactiae hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid degradation Streptococcus pneumoniae hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid highly specific for hyaluronan, degradation, unsaturated products of varied size Streptomyces hyalurolyticus hyaluronic acid oligomers
-
 ?
4.2.2.1 hyaluronic acid highly specific for hyaluronan Streptomyces hyalurolyticus hyaluronic acid oligomers primarily disaccharides, but also tetrasaccharides and hexasaccharides ?
4.2.2.1 additional information the enzyme also catalyzes the degradation of other polymeric glycans Streptococcus agalactiae ?
-
 ?
4.2.2.1 additional information the enzyme also catalyzes the degradation of other polymeric glycans Streptococcus pneumoniae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.35 More three-dimensional structure analysis Bos taurus
3.2.1.35 More three-dimensional structure analysis Apis mellifera
3.2.1.35 More three-dimensional structure analysis and modeling of isozymes, structure-reaction mechanism relationship, overview Homo sapiens
4.2.2.1 More domain structure, overview Streptomyces hyalurolyticus
4.2.2.1 More 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 Streptococcus agalactiae
4.2.2.1 More 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 Streptococcus pneumoniae
4.2.2.1 More the enzyme is very short in sequence and different in structure compared to enzymes of other species Streptococcus pyogenes phage H4489A

Synonyms

EC Number Synonyms Comment Organism
3.2.1.35 BPH-20
-
 Bos taurus
3.2.1.35 HPH-20
-
 Homo sapiens
3.2.1.35 human PH-20
-
 Homo sapiens
3.2.1.35 Hyal
-
 Homo sapiens
3.2.1.35 hyaluronidase
-
 Mus musculus
3.2.1.35 hyaluronidase
-
 Homo sapiens
3.2.1.35 hyaluronidase
-
 Bos taurus
3.2.1.35 hyaluronidase
-
 Apis mellifera
3.2.1.35 SPAM1
-
 Homo sapiens
3.2.1.35 spreading factor
-
 Homo sapiens
4.2.2.1 Hyal
-
 Streptococcus agalactiae
4.2.2.1 Hyal
-
 Streptococcus pneumoniae
4.2.2.1 Hyal
-
 Streptococcus pyogenes phage H4489A
4.2.2.1 HylP
-
 Streptococcus pyogenes phage H4489A
4.2.2.1 More the enzyme belongs to the CAZY polysaccharide lyase family 16 Streptococcus pyogenes phage H4489A
4.2.2.1 More the enzyme belongs to the polysaccharide lyase family 8 Streptococcus agalactiae
4.2.2.1 More the enzyme belongs to the polysaccharide lyase family 8 Streptococcus pneumoniae