Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.2.1 - hyaluronate lyase and Organism(s) Cutibacterium acnes and UniProt Accession P0CZ00

for references in articles please use BRENDA:EC4.2.2.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.1 hyaluronate lyase
IUBMB Comments
The enzyme catalyses the degradation of hyaluronan by a beta-elimination reaction. 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
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Cutibacterium acnes
UNIPROT: P0CZ00 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Cutibacterium acnes
The enzyme appears in selected viruses and cellular organisms
Synonyms
hyaluronate lyase, mucinase, hylp2, hyaluronan lyase, bacterial hyaluronidase, hyaluronidase sd, ha lyase, spnhl, hylb4755, acidic hyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucuronoglycosaminoglycan lyase
-
-
-
-
hyaluronidase
-
-
-
-
HYase
-
-
-
-
lyase, glucuronoglycosaminoglycan
-
-
-
-
lyase, hyaluronate
-
-
-
-
mucinase
-
-
-
-
spreading factor
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[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
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
hyaluronate lyase
The enzyme catalyses the degradation of hyaluronan by a beta-elimination reaction. 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
CAS REGISTRY NUMBER
COMMENTARY hide
37259-53-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chondroitin 4-sulfate
?
show the reaction diagram
-
weak activity
-
-
?
chondroitin 6-sulfate
?
show the reaction diagram
-
weak activity
-
-
?
hyaluronate
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
show the reaction diagram
eliminative reaction, degradation
-
-
?
hyaluronate
alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
phylogenetic analysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
phylogenetic analysis
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
bacterium employs two distinct variants of hyaluronan lyases. Variant HYL-IB/II is highly active, resulting in complete hyaluronan degradation. It is present in strains of the phylotypes IB and II. Variant HYL-IA has low activity, resulting in incomplete hyaluronan degradation. It is present in type IA strains. Type IA strains are primarily found on the skin surface and associated with acne vulgaris, type IB/II strains are more often associated with soft and deep tissue infections
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HYSA_CUTAC
812
0
87758
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
126000
-
x * 126000, SDS-PAGE
82000
x * 82000, amino acid sequence calculation
85110
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
-
37°C, 1 h, 80% loss of activity
210736
5 - 5.8
-
37°C, 1 h, stable
210736
7
-
37°C, 1 h, 70% loss of activity
210736
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
pH 5.8, 15 min, complete inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ingham, E.; Holland, K.T.; Gowland, G.; Cunliffe, W.J.
Purification and partial characterization of hyaluronate lyase (EC 4.2.2.1) from Propionibacterium acnes
J. Gen. Microbiol.
115
411-418
1979
Cutibacterium acnes
Manually annotated by BRENDA team
Steiner, B.; Romero-Steiner, S.; Cruce, D.; George, R.
Cloning and sequencing of the hyaluronate lyase gene from Propionibacterium acnes
Can. J. Microbiol.
43
315-321
1997
Cutibacterium acnes
Manually annotated by BRENDA team
Cove, J.H.; Holland, K.T.; Cunliffe, W.J.
Effects of oxygen concentration on biomass production, maximum specific growth rate and extracellular enzyme production by three species of cutaneous propionibacteria grown in continuous culture
J. Gen. Microbiol.
129
3327-3334
1983
Cutibacterium acnes, Cutibacterium granulosum
Manually annotated by BRENDA team
Hynes, W.L.; Walton, S.L.
Hyaluronidases of Gram-positive bacteria
FEMS Microbiol. Lett.
183
201-207
2000
Aeromonas sp., Bacteroides fragilis, Bacteroides ovatus, Candida albicans, Candida parapsilosis, Candida tropicalis, Clostridioides difficile, Clostridium chauvoei, Clostridium perfringens (P26831), Clostridium septicum, Cutibacterium acnes (P0CZ01), Cutibacterium granulosum, Fusobacterium mortiferum, Meyerozyma guilliermondii, Phocaeicola vulgatus, Pichia kudriavzevii, Porphyromonas asaccharolytica, Prevotella melaninogenica, Staphylococcus aureus (Q59801), Staphylococcus hyicus, Streptococcus agalactiae (O86478), Streptococcus constellatus, Streptococcus dysgalactiae, Streptococcus equi, Streptococcus intermedius, Streptococcus pneumoniae (Q54873), Streptococcus pyogenes, Streptococcus uberis, Streptomyces coelicolor, Streptomyces griseus (Q9WXL3), Streptomyces hyalurolyticus, Treponema pallidum, Treponema pallidum subsp. pertenue
Manually annotated by BRENDA team
Nazipi, S.; Stodkilde-Jorgensen, K.; Scavenius, C.; Brueggemann, H.
The skin bacterium Propionibacterium acnes employs two variants of hyaluronate lyase with distinct properties
Microorganisms
5
57
2017
Cutibacterium acnes
Manually annotated by BRENDA team