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Literature summary for 3.5.1.28 extracted from

  • Mellroth, P.; Karlsson, J.; Steiner, H.
    A scavenger function for a Drosophila peptidoglycan recognition protein (2003), J. Biol. Chem., 278, 7059-7064.
    View publication on PubMed
Search for more literature for 3.5.1.28

Cloned(Commentary)

Cloned (Comment) Organism
gene PGRP-SB1, expression of His6-tagged wild-type and mutant enzyme Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
C168A site-directed mutagenesis, the mutant is enzymatically inactive but retains its peptidoglycan affinity Drosophila melanogaster
C168S site-directed mutagenesis, the mutant is enzymatically inactive but retains its peptidoglycan affinity Drosophila melanogaster

Inhibitors

Inhibitors Comment Organism Structure
teichoic acid
-
 Drosophila melanogaster

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ absolutely required for activity, mutant PGRP-SC1B lacking a potential zinc ligand is enzymatically inactive but retains its peptidoglycan affinity Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetylmuramoyl-L-alanine + H2O Drosophila melanogaster the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, the immunostimulatory properties of PGRP-SC1B-degraded peptidoglycan are highly reduced N-acetylmuramate + L-alanine
-
 ?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q70PY2 gene PGRP-SB1 or CG9681; gene PGRP-SB1 or CG9681
-

Purification (Commentary)

Purification (Comment) Organism
gene PGRP-SB1, recombinant His6-tagged wild-type and mutant enzyme by nickel affinity chromatography Drosophila melanogaster

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 the enzyme shows highest activity with peptidoglycan substrates from Staphylococcus aureus, and 34% and 23% of this activity with substrate from Micrococcus luteus and Bacillus megaterium, respectively, at pH 8.0 Drosophila melanogaster

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme does not show antibacterial activity Drosophila melanogaster ?
-
 ?
N-acetylmuramoyl-L-alanine + H2O the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, the immunostimulatory properties of PGRP-SC1B-degraded peptidoglycan are highly reduced Drosophila melanogaster N-acetylmuramate + L-alanine
-
 ?
N-acetylmuramoyl-L-alanine + H2O the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, peptidoglycan substrates from Staphylococcus aureus, Micrococcus luteus, and Bacillus megaterium, the enzyme hydrolyzes the lactylamide bond between the glycan strand and the cross-linking peptides, analysis of the cleavage products by mass spectrometry Drosophila melanogaster N-acetylmuramate + L-alanine
-
 ?

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the peptidoglycan recognition protein, PGRP, family Drosophila melanogaster
PGRP-SB1
-
 Drosophila melanogaster

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22 25 assay at Drosophila melanogaster

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8 assay at Drosophila melanogaster