Literature summary extracted from
Kang, M.S.; Elango, N.; Mattia, E.; Au-Young, J.; Robbins, P.W.; Cabib, E.
Isolation of chitin synthetase from Saccharomyces cerevisiae. Purification of an enzyme by entrapment in the reaction product (1984), J. Biol. Chem., 259, 14966-14972.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.4.1.16 |
GlcNAc |
- |
Saccharomyces cerevisiae |
|
General Stability
EC Number |
General Stability |
Organism |
---|
2.4.1.16 |
upon lyophilization, about 70% of the activity is recovered |
Saccharomyces cerevisiae |
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
2.4.1.16 |
0.7 |
- |
UDP-GlcNAc |
- |
Saccharomyces cerevisiae |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
2.4.1.16 |
570000 |
- |
gel filtration, calculation from sedimentation coefficient |
Saccharomyces cerevisiae |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.4.1.16 |
Saccharomyces cerevisiae |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.4.1.16 |
- |
Saccharomyces cerevisiae |
Storage Stability
EC Number |
Storage Stability |
Organism |
---|
2.4.1.16 |
-80°C, quite stable for several months |
Saccharomyces cerevisiae |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.4.1.16 |
UDP-N-acetyl-D-glucosamine + [1,4-(N-acetyl-beta-D-glucosaminyl)]n |
the enzyme itself is capable both of initiating chitin chains without a primer and of determining their length |
Saccharomyces cerevisiae |
UDP + [1,4-(N-acetyl-beta-D-glucosaminyl)]n+1 |
at low concentrations of UDP-GlcNAc, no insoluble chitin is formed. Instead N-acetylglucosamine is incorporated into water-soluble products |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.4.1.16 |
More |
in SDS-PAGE, the purified enzyme shows a major band of 63000 Da and a weaker band at 74000 Da |
Saccharomyces cerevisiae |