EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.4.1.129 | more |
the enzyme possesses peptidoglycan transglycosylase activity that lacks penicillin-binding activity |
Streptococcus pneumoniae |
? |
- |
? |
2.4.1.129 | more |
the enzyme shows both transglycosylase and transpeptidase activities |
Escherichia coli |
? |
- |
? |
2.4.1.129 | more |
overproduction of the inactive PBP1B variants causes lysis of wild-type cells |
Escherichia coli |
? |
- |
? |
2.4.1.129 | more |
penicillin-binding protein 1b is the key enzyme responsible for the formation of the polysaccharide backbone of the peptidoglycan as well as for cross-linking of its peptide portion |
Escherichia coli |
? |
- |
? |
2.4.1.129 | more |
dimerized enzyme synthesizes murein with long glycan strands of an average length of more than 25 disaccharide units with almost 50% of the peptides being part of cross-links. PBP1B is also capable of synthesizing trimeric muropeptide structures |
Escherichia coli |
? |
- |
? |
2.4.1.129 | more |
penicillin binding protein 1b has transglycosylase and transpeptidase activity |
Escherichia coli |
? |
- |
? |
2.4.1.129 | more |
the penicillin-binding protein 1B is a bifunctional murein synthase containing both a transpeptidase domain and a transglycosylasedomain, The protein is present in three forms: alpha, beta and gamma |
Escherichia coli |
? |
- |
? |
2.4.1.129 | more |
utility of Lipid II and Lipid IV substrates to probe the mechanism of the enzyme |
Escherichia coli |
? |
- |
? |
2.4.1.129 | more |
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present |
Staphylococcus aureus |
? |
- |
? |
2.4.1.129 | more |
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present |
Escherichia coli |
? |
- |
? |