Gametolysin | |||||||||
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Identifiers | |||||||||
EC number | 3.4.24.38 | ||||||||
CAS number | 97089-74-2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Search | |
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PMC | articles |
PubMed | articles |
NCBI | proteins |
An autolysin is an enzyme (EC 3.4.24.38, gametolysin, Chlamydomonas cell wall degrading protease, lysin, Chlamydomonas reinhardtii metalloproteinase, gamete lytic enzyme, gamete autolysin) that hydrolyzes (and breaks down) the components of a biological cell or a tissue in which it is produced. It is similar in function to a lysozyme. This enzyme catalyses the following chemical reaction
This glycoprotein is present in Chlamydomonas reinhardtii gametes.
Autolysins exist in all bacteria containing peptidoglycan. The peptidoglycan matrix is very rigid, so these enzymes break down the peptidoglycan matrix in small sections so that growth and division of cells can occur. Autolysins do this by hydrolyzing the β-(1,4) bond between N-acetylmuramic acid and N-acetylglucosamine molecules. Autolysins are naturally produced by peptidoglycan containing bacteria, but excessive amounts will degrade the peptidoglycan matrix and cause the cell to burst due to osmotic pressure. Gram-positive bacteria regulate autolysins with teichoic acid molecules attached to the tetrapeptide of the peptidoglycan matrix.