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Record W2911890499 · doi:10.22215/etd/2015-10900

INVESTIGATION OF THE CATALYTIC AND REGULATORY DOMAINS OF CYSTATHIONINE β-SYNTHASE

2015· dissertation· en· W2911890499 on OpenAlexaff
Edgar Abouassaf

Bibliographic record

Venuenot available
Typedissertation
Languageen
FieldMedicine
TopicFolate and B Vitamins Research
Canadian institutionsCarleton University
Fundersnot available
KeywordsCystathionine beta synthaseActive siteChemistryStereochemistryBiochemistryCofactorHomocystinuriaBinding siteConformational changeResidue (chemistry)TryptophanSerineEnzymeCysteineAmino acidMethionine

Abstract

fetched live from OpenAlex

Cysthationine β-Synthase (CBS) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the condensation of serine and homocysteine to form cysthathionine.Human CBS (hCBS) is a modular enzyme that contains an N-terminal domain that binds heme, a catalytic domain that binds the PLP cofactor and a regulatory domain that binds S-adenosyl-methionine (SAM).The interaction between the catalytic and regulatory regions is limited to a linker region that forms the main communication between these two domains.Deficiency in CBS activity is the leading cause for the disorder homocystinuria in humans.The focus of the studies described in this thesis is to investigate the mechanism of homocystinuria-associated mutations in the active site of yeast CBS, the potential of native tryptophan residues as probes of conformational change and the binding of SAM to the regulatory domain.Site-directed replacement variants of 9 residues located in the active-site of the truncated form of yeast CBS (residues 1-353) were characterized.The results suggest that the hydrogen bonding network comprising residues K112, E111, K327, E244 and T326 is a determinant of active-site architecture and dynamics.Residues G245, I246 and G247, situated adjacent to the cofactor, play a role in maintaining PLP in a catalytically productive orientation.With the goal of developing probes of conformational change within the catatlytic domain and of communication between the catalytic and regulatory domain of CBS, single and triple-substitution, site-directed variants of the four tryptophan residues of yeast CBS (W132, W263, W333 and W340) were characterized in the truncated and fulllength enzyme forms.Residues W132 and W263 are located in the active site, while iii W333 and W340 are located in the linker region that connects the catalytic and regulatory domains.The results demonstrate that residue W263 is the main contributor for fluorescence resonance energy transfer to the PLP cofactor.Substitution of W333 and W340 causes a change in the degree of solvent exposure in the microenvironment of these residues.This is due to the presence of the regulatory domain in the full-length enzyme.Binding of SAM to the regulatory domain of human CBS leads to enzyme activation.In contrast, the Drosophila melanogaster and yeast CBS enzymes are not activated by SAM.The binding of SAM to the regulatory domains of yeast and human CBS was investigated via fluorescence spectroscopy and mass spectrometry.The results indicate that the full-length yeast enzyme does not bind to SAM, suggesting that, similar to the drosophila enzyme, yeast CBS may locked in a conformation that does not allow SAM-binding to its regulatory domain.

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 machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: metacan-v3-hybrid-931329e0061cValidation 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 score0.001
Threshold uncertainty score0.003

Distilled classifier scores by category (both heads)

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)0.0010.000

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 head0.029
GPT teacher head0.312
Teacher spread0.282 · 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 source (direct Gemma or distilled Codex), 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

Citations0
Published2015
Admission routes1
Has abstractyes

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