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Record W1989171083 · doi:10.1021/bi051679s

Identification and Characterization of <i>O</i>-Acetylpeptidoglycan Esterase:  A Novel Enzyme Discovered in <i>Neisseria gonorrhoeae</i>

2005· article· en· W1989171083 on OpenAlexaff
Joel T. Weadge, Anthony J. Clarke

Bibliographic record

VenueBiochemistry · 2005
Typearticle
Languageen
FieldMedicine
TopicPeptidase Inhibition and Analysis
Canadian institutionsUniversity of Guelph
Fundersnot available
KeywordsNeisseria gonorrhoeaeMicrobiologyEnzymeEsteraseIdentification (biology)ChemistryBiologyComputational biologyBiochemistry

Abstract

fetched live from OpenAlex

Modification of the bacterial cell wall heteropolymer peptidoglycan by addition of an acetyl group to the C-6 hydroxyl group of N-acetylmuramoyl residues is known to inhibit the activity of muramidases (lysozymes) of innate immune systems. The O-acetylation of peptidoglycan also precludes the action of intrinsic lytic transglycosylases, enzymes that require a free C-6 hydroxyl group to generate their 1,6-anhydromuropeptide products. This class of autolysins is ubiquitous in peptidoglycan-synthesizing bacteria as they are responsible for insertion of pores and flagella, spore formation, and the general metabolism of peptidoglycan. We recently discovered a cluster of genes in the Neisseria gonorrhoeae chromosome that are proposed to participate in peptidoglycan O-acetylation (Weadge, J. T., Pfeffer, J. M., and Clarke, A. J. (2005) BMC Microb. 5, 49). In the current study, we demonstrate that one of these genes, ape1 functions as an O-acetylpeptidoglycan esterase. The ape1 gene was cloned and overexpressed in Escherichia coli as a fusion protein with a hexa-histidine tag. The expressed protein was purified to apparent homogeneity and assayed for activity as an esterase using three different assays involving high-performance liquid chromatography and chromogenic detection methods which measured the release of ester-linked acetate from a variety of polymer and soluble substrates. These assays demonstrated that Ape1 has a higher specific activity on O-acetylated peptidoglycan compared to O-acetylated xylan. Consequently, Ape1 represents the first enzyme characterized as an O-acetylpeptidoglycan esterase. The physicochemical and kinetic parameters of Ape1 were determined using soluble chromogenic substrates for convenience. Thus, its pH optima for stability and activity were observed to be 6.0 and 6.2, respectively, while its optimum temperature for activity was 55 degrees C. Two forms of truncated Ape1 are generated in E. coli, one lacked the complete predicted N-terminal signal sequence, while the second involved a proteolytic cleavage within this signal sequence. The smaller truncated form was localized predominantly to the periplasm, whereas the larger form was mainly associated with the outer membrane, and to a lesser extent, the cytoplasmic membrane, sites expected for the maintenance of peptidoglycan.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.015
Threshold uncertainty score0.423

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.007
GPT teacher head0.242
Teacher spread0.234 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations57
Published2005
Admission routes1
Has abstractyes

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