2.4.1.212: hyaluronan synthase
This is an abbreviated version!
For detailed information about hyaluronan synthase, go to the full flat file.
Word Map on EC 2.4.1.212
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2.4.1.212
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glycosaminoglycans
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collagen
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polysaccharide
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keratinocytes
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cartilage
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4-methylumbelliferone
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proteoglycans
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hyaluronidases
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chondrocytes
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dermal
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mesenchymal
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pericellular
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pasteurella
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udp-glucuronic
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hyals
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versican
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cumulus
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synovial
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vocal
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articular
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aggrecan
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osteoarthritis
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streptococcal
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udp-n-acetylglucosamine
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multocida
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rhamm
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pyogenes
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udp-sugars
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chondroitin
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glucuronic
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procollagen
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synoviocytes
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cumulus-oocyte
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decorin
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udp-glcua
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photoaging
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filaggrin
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equisimilis
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ha-binding
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temporomandibular
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glcua
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perineuronal
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ophthalmopathy
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zooepidemicus
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uvb-irradiated
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ha-mediated
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tnfaip6
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medicine
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hyaluronan-binding
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fibromodulin
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biglycan
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analysis
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synthesis
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drug development
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biotechnology
- 2.4.1.212
- glycosaminoglycans
- collagen
- polysaccharide
- keratinocytes
- cartilage
- 4-methylumbelliferone
- proteoglycans
- hyaluronidases
- chondrocytes
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dermal
- mesenchymal
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pericellular
- pasteurella
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udp-glucuronic
-
hyals
- versican
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cumulus
- synovial
-
vocal
-
articular
- aggrecan
- osteoarthritis
- streptococcal
- udp-n-acetylglucosamine
- multocida
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rhamm
- pyogenes
- udp-sugars
- chondroitin
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glucuronic
- procollagen
- synoviocytes
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cumulus-oocyte
- decorin
- udp-glcua
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photoaging
- filaggrin
- equisimilis
-
ha-binding
-
temporomandibular
-
glcua
-
perineuronal
- ophthalmopathy
- zooepidemicus
-
uvb-irradiated
-
ha-mediated
-
tnfaip6
- medicine
-
hyaluronan-binding
- fibromodulin
- biglycan
- analysis
- synthesis
- drug development
- biotechnology
Reaction
Synonyms
CHAS2, CHAS3, class I hyaluronan synthase, CPS1, DG42 protein, HA synthase, HA synthase 3, HA1, HA2, HA3, HAS, HAS-1, HAS-2, HAS-3, HAS1, Has2, Has3, hasA, HASs, HsHAS1, HuHAS1, HyaD, hyaluronan synthase, hyaluronan synthase 1, hyaluronan synthase 2, hyaluronan synthase 3, hyaluronan synthase-1, hyaluronan synthase-2, hyaluronan synthases 2, hyaluronan synthethase, hyaluronate synthase, hyaluronate synthetase, hyaluronic acid synthase, hyaluronic acid synthetase, More, PmHAS, seHAS, XHAS1, XHAS2, XHAS3
ECTree
2.4.1.212 hyaluronan synthaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.4.1.212 - hyaluronan synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S221A
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site-directed mutation of the O-GlcNAcylable Ser-221 to alanine generated an enzyme with a calculated t1/2 of about 70 min
T110A
site-directed mutagenesis of the phosphorylation site residue, the mutant is not inhibited by AMP-activated protein kinase
K190R
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site-directed mutagenesis, inactive mutant, K190R-mutated HAS2 forms dimers with wild-type HAS2 and quenches the activity of wild-type HAS2
D247E
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D247K
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D247N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D249E
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D249K
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D249N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
D370E
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low hyaluronan synthase activity
D370K
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
D370N
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
D477K
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mutants possess UDP-N-acetyl-D-glucosamine-transferase activity
D527E
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
D527K
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
D527N
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
D529E
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site-directed mutagenesis, mutant possesses GlcNAc-transferase activity, and low hyaluronan synthase activity
D529K
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site-directed mutagenesis, mutant possesses GlcNAc-transferase activity, and very low hyaluronan synthase activity
D529N
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site-directed mutagenesis, mutant possesses only GlcNAc-transferase activity
E369D
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
E369H
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
E369Q
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site-directed mutagenesis, mutant possesses GlcUA-transferase activity, and very low GlcNAc-transferase activity
D247E
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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D247K
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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D247N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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D249N
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site-directed mutagenesis, mutant possesses only GlcUA-transferase activity
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C226A
C226A/C262A
C226A/C262A/C367A
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site-directed mutagenesis, 1.4% remaining activity and altered kinetic constants compared to the wild-type enzyme
C226A/C281A
C226A/C367A
C226S
C262A
C262A/C281A
C262A/C367A
C262S
C281A
C281A/C367A
C281S
C367A
C367S
delD409-L417
deletion of 409-DWGTRKKLL-417 causes significant decreases in hyaluronic acid titer and in vitro hyaluronan synthase activity and undetectable hyaluronic acid weight-average molecular weight. Stepping truncations from L417 to K415 have little impact on hyaluronic acid and molecular weight. The removal of L417-K414, the hyaluronic acid titer of the resulting WGTR413 variant dramatically decreased to 16.8% of the wild type, while the same hyaluronic acid molecular weight is still detectable. With the further removal of R413, the hyaluronic acid titer of the resulting WGT412 variant dropps to less than 10% of the wild-type, and no hyaluronic acid products are detectable
E327D
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the specific enzyme activity relative to wild type enzyme is 38%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
E327K
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the specific enzyme activity relative to wild type enzyme is 0.16%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
E327K/K48E
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the specific enzyme activity near wild-type level. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzymel
E327Q
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the specific enzyme activity relative to wild type enzyme is 26%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
K414A
mutation does not notably affect hyaluronic acid titer
K414R
mutation does not notably affect hyaluronic acid titer. The molecular weight of the hyaluronic acid produced by the K414R variant is significantly increased
K415A
mutation does not notably affect hyaluronic acid titer
K415R
mutation does not notably affect hyaluronic acid titer
K48E
K48F
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site-directed mutagenesis, alteration of K48 within membrane domain 2 causes decreased activity and HA product size
K48R
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the specific enzyme activity relative to wild type enzyme is 17%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
R406A
hyaluronic acid titer is greatly decreased
R413A
hyaluronic acid titer is greatly decreased
R413K
the variant barely produces hyaluronic acid
T412A
mutations completely deactivates the enzyme
W410A
mutations completely deactivates the enzyme
N196I/L197R/T202S/D203H/C226F/S231D/V232F/E236Q/S256N/C262S/K294T/N297H/N300K/F303C
the enzyme is engineered to increase hyaluronan production and molecular mass through structural alteration of multiple regions. As compared with other variants and wild-type enzyme, the V5 variant generates a higher hyaluronan titer (2.24 g/l) and molecular weight value (1360000 Da). Following overexpression of the genes tuaD and glmU in Bacillus subtilis V5, hyaluronan production and molecular weight increases further to 2.81 g/l and 2430000 Da, respectively. The results provide a new strategy for producing hyaluronan with higher titers and molecular mass values that could be extended to other polysaccharides, such as heparosan and chondroitin, produced in Bacillus subtilis
C117L
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C117S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C210S
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C239S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C239S/C337S
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site-directed mutagenesis, reduced recombinant expression level, activity is similar to the wild-type enzyme
C298F
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site-directed mutagenesis, poor recombinant expression level, highly reduced activity compared to the wild-type enzyme
C298L
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site-directed mutagenesis, poor recombinant expression level, highly reduced activity compared to the wild-type enzyme
C298S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C304S
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site-directed mutagenesis, activity is similar to the wild-type enzyme
C304S/C337S
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C307S
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
C307S/C337S
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site-directed mutagenesis, reduced recombinant expression level, inactive mutant
C337S
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site-directed mutagenesis, increased Km for UDP-N-acetylglucosamine compared to the wild-type enzyme
additional information
C226A
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site-directed mutagenesis, 24% remaining activity and altered kinetic constants compared to the wild-type enzyme
C226A
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site-directed mutagenesis, increased sensitivity to inhibition by NEM
C226A
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site-directed mutagenesis, the mutant shows 44% of wild-type activity
C226A/C262A
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site-directed mutagenesis, 3.2% remaining activity and altered kinetic constants compared to the wild-type enzyme
C226A/C262A
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site-directed mutagenesis, slightly increased sensitivity to inhibition by NEM, and reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C226A/C262A
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site-directed mutagenesis, the mutant shows 36% of wild-type activity, mutant kinetics compared to the wild-type enzyme
C226A/C281A
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site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C226A/C281A
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site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C226A/C281A
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site-directed mutagenesis, the mutant shows 68% of wild-type activity
C226A/C367A
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site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C226A/C367A
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site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and slightly increased sensitivity to inhibition by sodium arsenite compared to the wild-type
C226A/C367A
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site-directed mutagenesis, the mutant shows 102% of wild-type activity
C226S
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site-directed mutagenesis, highly reduced reaction velocity and altered Km values compared to the wild-type enzyme
C226S
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site-directed mutagenesis, reduced sensitivity to inhibition by NEM
C226S
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site-directed mutagenesis, the mutant shows 45% of wild-type activity, mutant kinetics compared to the wild-type enzyme
C262A
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site-directed mutagenesis, increased sensitivity to inhibition by NEM
C262A
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site-directed mutagenesis, reduced reaction velocity and increased Km values compared to the wild-type enzyme
C262A
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site-directed mutagenesis, the mutant shows 79% of wild-type activity
C262A/C281A
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site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C262A/C281A
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site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C262A/C281A
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site-directed mutagenesis, the mutant shows 82% of wild-type activity, mutant kinetics compared to the wild-type enzyme
C262A/C367A
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site-directed mutagenesis, increased sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C262A/C367A
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site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C262S
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site-directed mutagenesis, increased sensitivity to inhibition by NEM
C262S
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site-directed mutagenesis, reduced reaction velocity and increased Km values compared to the wild-type enzyme
C262S
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site-directed mutagenesis, the mutant shows 85% of wild-type activity
C281A
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site-directed mutagenesis, highly reduced sensitivity to inhibition by NEM
C281A
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site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C281A
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site-directed mutagenesis, the mutant shows 91% of wild-type activity
C281A/C367A
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site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C281A/C367A
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site-directed mutagenesis, reduced sensitivity to inhibition by NEM, and highly reduced sensitivity to inhibition by sodium arsenite compared to the wild-type enzyme
C281A/C367A
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site-directed mutagenesis, the mutant shows 107% of wild-type activity
C281S
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site-directed mutagenesis, increased sensitivity to inhibition by NEM
C281S
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site-directed mutagenesis, reduced reaction velocity and altered Km values compared to the wild-type enzyme
C281S
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site-directed mutagenesis, the mutant shows 57% of wild-type activity
C367A
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site-directed mutagenesis, increased reaction velocity and Km values compared to the wild-type enzyme
C367A
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site-directed mutagenesis, unaltered inhibition by NEM compared to the wild-type enzyme
C367A
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site-directed mutagenesis, the mutant shows 126% of wild-type activity
C367S
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site-directed mutagenesis, kinetics similar to the wild-type enzyme
C367S
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site-directed mutagenesis, unaltered inhibition by NEM compared to the wild-type enzyme
C367S
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site-directed mutagenesis, the mutant shows 80% of wild-type activity
K48E
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the specific enzyme activity relative to wild type enzyme is 7%. Mutant enzyme synthesizes hyaluronan of smaller weight-average molar mass than wild-type enzyme
K48E
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site-directed mutagenesis, alteration of K48 within membrane domain 2 causes decreased activity and HA product size
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
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COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has1 isozyme. HAS1 is almost unable to secrete hyaluronan or form a hyaluronan coat. This failure of HAS1 to synthesize hyaluronan is compensated by increasing the cellular content of UDP-GlcNAc by 10fold with 1 mM glucosamine in the growth medium
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
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COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has2 isozyme. Hyaluronan synthesis driven by HAS2 is less affected by glucosamine addition
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
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COS-1 cells, with minor endogenous hyaluronan synthesis, is transfected with Has3 isozyme. The ability of HAS3 to synthesize hyaluronan is not at all affected
additional information
both COS-1 and MCF-7 cell lines have negligible endogenous hyaluronan production, and even overexpression of HAS1 enzymes does not cause prominent changes in it. Upon treatment with glucose or glucosamine, compounds that increase the amounts of hyaluronan substrates, the HAS1 enzyme is able to produce significant amounts of hyaluronan
additional information
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HAS1-transfected MCF-7cells show very little cell surface hyaluronan, but a large hyaluronan coat is seen in cells grown in 20 mM glucose and 1 mM glucosamine, or treated with interleukin-1beta, TNF-alpha, or TGF-beta. The coats are mostly removed by the presence of hyaluronan hexasaccharides, or Hermes1 antibody, indicating that they depend on the CD44 receptor, which is, in contrast to the coat produced by HAS3, remaining attached to HAS3 itself
additional information
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isozyme HAS3 overexpression expands the cell surface hyaluronan coat and decreases melanoma cell adhesion, migration and proliferation by cell cycle arrest at G1/G0. Melanoma cell migration is restored by removal of cell surface hyaluronan by Streptomyces hyaluronidase and by receptor blocking with hyaluronan oligosaccharides, while the effect on cell proliferation is receptor independent. Overexpression of isozyme HAS3 decreases ERK1/2 phosphorylation suggesting that inhibition of MAP-kinase signaling is responsible for the suppressive effects on the malignant phenotype of MV3 melanoma cells
additional information
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site-directed mutagenesis of residues of the cytoplasmic loop of isozyme HAS1 for determining the residues required for glycosyltransferase activity
additional information
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activity rescue of mutants with high substrate concentrations, overview, deletion of residues 1-117 does not affect polymerization activity, construction of different chimeric mutant enzymes comprising residues from Pasteurella multocida type A enzyme and residues of a Pasteurella multocida type F chondroitin synthase, producing an unsulfated chondroitin capsule, the chimeric mutants show different percentages of hyaluronan and chondroitin synthase ativities, overview
additional information
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a truncated soluble form of recombinant PmHAS (residues 1703) can catalyze the glycosyl transfers in a time- and concentration-dependent manner
additional information
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activity rescue of mutants with high substrate concentrations, overview, deletion of residues 1-117 does not affect polymerization activity, construction of different chimeric mutant enzymes comprising residues from Pasteurella multocida type A enzyme and residues of a Pasteurella multocida type F chondroitin synthase, producing an unsulfated chondroitin capsule, the chimeric mutants show different percentages of hyaluronan and chondroitin synthase ativities, overview
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additional information
expression of isozyme HAS1 is increased after oncogenic malignant transformation with v-sre and/or v-fos, no increase after transformation with v-HA-ras, introduction of isozyme HAS1 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS1 is increased after oncogenic malignant transformation with v-sre and/or v-fos, no increase after transformation with v-HA-ras, introduction of isozyme HAS1 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS1 is increased after oncogenic malignant transformation with v-sre and/or v-fos, no increase after transformation with v-HA-ras, introduction of isozyme HAS1 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS2 is increased after oncogenic malignant transformation with v-HA-ras, v-sre and/or v-fos, antisense repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum, introduction of isozyme HAS2 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS2 is increased after oncogenic malignant transformation with v-HA-ras, v-sre and/or v-fos, antisense repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum, introduction of isozyme HAS2 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
expression of isozyme HAS2 is increased after oncogenic malignant transformation with v-HA-ras, v-sre and/or v-fos, antisense repression of HAS2 expression leads to reduced hyaluronan synthesis and reduced tumorigenicity in the peritoneum, introduction of isozyme HAS2 promotes the growth of subcutaneous tumors dependent on hyaluronan synthesis level
additional information
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construction and kinetic analysis of Cys-deletion mutants, overview
additional information
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construction of cysteine-deletion mutants deleting either C226, C262, C281, or C367, the mutants are less sensitive or not sensisitive to sodium arsenite inhibition, overview
additional information
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addition of purified HAS to liposomes preloaded with the fluorophore Cascade Blue, CB, which is translocated through the membrane and secreted by HAS, overview. SeHAS-mediated CB efflux is greater from liposomes made with an activating lipid, tetraoleoyl cardiolipin, compared to an inactivating lipid, tetramyristoyl cardiolipin
additional information
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generation of several deletion mutants, DELTA3-C281, DELTA3-C226, DELTA3-C262, and DELTA3-C367, and of a C-null mutant, all show reduced activity and altered kinetics compared to the wild-type enzyme
additional information
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purified Se-HAS is reconstituted into proteoliposomes, from total lipid extract from Escherichia coli, where it synthesizes and translocates hyaluronan, or reconstituted into synthetic 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine/1,1',2,2'-tetraoleoyl cardiolipin/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (80/10/10%) proteoliposomes. In vitro synthesized, high-molecular-weight hyaluronan remains tightly associated with the intact proteoliposomes, even after proteolyticdegradation of HAS or in the presence of 1 M NaCl or 0.6 M urea to prevent nonspecific interactions of the polymer with the lipid vesicles
additional information
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dual expression of hyaluronan synthase and UDP-glucose-6-dehydrogenase in Lactococcus lactis and study of the ratios of hyaluronan synthase expression level to the precursor sugar UDP-GlcA biosynthesis ability under different induction concentration collocations with nisin and lactose on the molecular weight of hyaluronan. The final weight-average molecular weight of hyaluronan correlates with the relative ratios of hyaluronan synthase expression level to the concentration of UDP-GlcA
additional information
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dual expression of hyaluronan synthase and UDP-glucose-6-dehydrogenase in Lactococcus lactis and study of the ratios of hyaluronan synthase expression level to the precursor sugar UDP-GlcA biosynthesis ability under different induction concentration collocations with nisin and lactose on the molecular weight of hyaluronan. The final weight-average molecular weight of hyaluronan correlates with the relative ratios of hyaluronan synthase expression level to the concentration of UDP-GlcA
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