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Literature summary for 3.5.1.28 extracted from

  • Fernandez-Tornero, C.; Garcia, E.; Lopez, R.; Gimenez-Gallego, G.; Romero, A.
    Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer (2002), J. Mol. Biol., 321, 163-173.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
lytA gene, expression in Escherichia coli RB791 Streptococcus pneumoniae

Crystallization (Commentary)

Crystallization (Comment) Organism
two crystal forms of the C-terminal cell wall anchoring/choline-binding domain of LytA Streptococcus pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface LytA is a surface-exposed enzyme Streptococcus pneumoniae 9986
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36600
-
 2 * 36600, catalytically active homodimer, dimer interface Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peptidoglucan + H2O Streptococcus pneumoniae cell autolysis, LytA rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone, LytA is an important pneumococcal virulence factor ?
-
 ?

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae P06653
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant LytA Streptococcus pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptidoglucan + H2O cell autolysis, LytA rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone, LytA is an important pneumococcal virulence factor Streptococcus pneumoniae ?
-
 ?
peptidoglucan + H2O LytA structure, 36.6 kDa modular enzyme comprising an N-terminal catalytic domain plus the C-terminal choline-binding domain, the former catalyzes the hydrolysis of the N-acetylmuramoyl-L-alanine bond present in the pneumococcal peptidoglycan backbone, fundamental role of the 11 C-terminal residues in the catalytic activity of LytA Streptococcus pneumoniae ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 36600, catalytically active homodimer, dimer interface Streptococcus pneumoniae
monomer monomeric LytA retains less than 10% of activity compared with the active homodimeric enzyme Streptococcus pneumoniae

Synonyms

Synonyms Comment Organism
LytA major autolysin of Streptococcus pneumoniae Streptococcus pneumoniae