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Literature summary for 3.5.1.28 extracted from

  • Patel, J.G.; Narra, H.P.; Sepuru, K.M.; Sahni, A.; Golla, S.R.; Sahni, A.; Singh, A.; Schroeder, C.L.C.; Chowdhury, I.H.; Popov, V.L.; Sahni, S.K.
    Evolution, purification, and characterization of RC0497 a peptidoglycan amidase from the prototypical spotted fever species Rickettsia conorii (2020), Biol. Chem., 401, 249-262c .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene RC0497, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Rickettsia conorii

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall predominantly Rickettsia conorii 5618
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cytoplasm
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Rickettsia conorii 5737
-
additional information the enzyme is predominantly located to the cell wall, septal regions of replicating bacteria, and the membrane of vesicles pinching off the cell wall Rickettsia conorii
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periplasm
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Rickettsia conorii
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vesicle
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Rickettsia conorii 31982
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ Zn2+-bound holoform, the enzyme exhibits conformational changes in the presence of zinc ion. Structural analysis of RC0497 reveals potential involvement of amino acid residues D53, H60, and H73 in binding to zinc Rickettsia conorii

Organism

Organism UniProt Comment Textmining
Rickettsia conorii Q92IC3
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-
Rickettsia conorii Malish 7 Q92IC3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Rickettsia conorii

Source Tissue

Source Tissue Comment Organism Textmining
additional information the single monolayer of microvascular endothelium lining the blood vessels represents the primary target of pathogenic Rickettsia species for establishment and dissemination of infection Rickettsia conorii
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide Rickettsia conorii ?
-
?
additional information the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide Rickettsia conorii Malish 7 ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 29500, about, mass spectrometry Rickettsia conorii
More N-acetylmuramoyl-L-alanine amidase family proteins are known to exist in solution as a mix of monomeric and dimer forms Rickettsia conorii

Synonyms

Synonyms Comment Organism
Peptidoglycan hydrolase
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Rickettsia conorii
PG amidase
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Rickettsia conorii
RC0497
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Rickettsia conorii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Rickettsia conorii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Rickettsia conorii

Expression

Organism Comment Expression
Rickettsia conorii N-acetylmuramoyl-L-alanine amidase is constitutively expressed during infection of cultured human microvascular endothelial cells at the levels of both mRNA transcript and encoded protein additional information

General Information

General Information Comment Organism
evolution two proteins, namely RC0497 and RC1358, belong to the AmpD superfamily containing an amidase_2 domain as defined in the Pfam database (PF01510) and potentially endowed with amidase activity, phylogenetic analysis. The PG_binding_1 domain is present only in RC0497 at the C-terminus, but missing in RC1358 Rickettsia conorii
metabolism higher enzymatic activity of RC0497 in peptidoglycan hydrolysis when compared to lysozyme Rickettsia conorii
additional information N-acetylmuramoyl-L-alanine amidase is constitutively expressed during infection of cultured human microvascular endothelial cells at the levels of both mRNA transcript and encoded protein Rickettsia conorii
physiological function RC0497 is a peptidoglycan hydrolase unique to spotted fever rickettsiae. The enzyme may potentially serve as moonlighting protein capable of performing multiple functions during host-pathogen interactions. RC0497 encoding the enzyme is highly expressed at the levels of both transcription and translation during Rickettsia conorii infection of cultured human microvascular endothelial cells (HMECs). Possibly RC0497 acts in association with RC1358 and AmpG aids in the breakdown of peptidoglycan (PG) fragments in the periplasm and their recycling to prevent activation of host immune responses. RC0497 may also interact with host components/proteins and play roles in facilitating the re-entry and spread of spotted fever group (SFG) rickettsiae during infection Rickettsia conorii