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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Localization

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.28 36600
-
 2 * 36600, catalytically active homodimer, dimer interface Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.28 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

EC Number Organism UniProt Comment Textmining
3.5.1.28 Streptococcus pneumoniae P06653
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.28 recombinant LytA Streptococcus pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.28 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 ?
-
 ?
3.5.1.28 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

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

Synonyms

EC Number Synonyms Comment Organism
3.5.1.28 LytA major autolysin of Streptococcus pneumoniae Streptococcus pneumoniae