Evidence map›Paper›PMID 41761765›Full record

ArticleProtein engineering, design & selection : PEDS2025

Expansion of the known poly(aspartic acid) hydrolases through the identification of four new PahZ1 homologs.

Justin D Marsee, Chad A Brambley, Thi Ho, Waylan W Callaway, Amanda L Jansch, Kaitlyn Taylor, Shelby R Watson-Sanders, Britney Williams, Austin Wolvington, Catherine T Nguyen and 6 more

Abstract read
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In one paragraph

Article in Protein engineering, design & selection : PEDS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors.

Justin D MarseeDepartment of Chemistry, Middle Tennessee State University, 1301 East Main Street, Murfreesboro, TN, 37132, United States.
Chad A BrambleyDepartment of Chemistry, Middle Tennessee State University, 1301 East Main Street, Murfreesboro, TN, 37132, United States.
Thi HoDepartment of Chemistry and Biochemistry, Georgia Southern University, 11935 Abercorn Street, Savannah, GA, 31419, United States.
Waylan W CallawayDepartment of Chemistry and Biochemistry, Georgia Southern University, 11935 Abercorn Street, Savannah, GA, 31419, United States.
Amanda L JanschDepartment of Chemistry and Biochemistry, Georgia Southern University, 11935 Abercorn Street, Savannah, GA, 31419, United States.
Kaitlyn TaylorDepartment of Chemistry, Indiana University, 212 S. Hawthorne Drive, Bloomington, IN, 47405, United States.
Shelby R Watson-SandersThe University of Tennessee, Department of Chemistry, 2641 Osprey Vista Way, Knoxville, TN 37920, United States.
Britney WilliamsDepartment of Chemistry, Middle Tennessee State University, 1301 East Main Street, Murfreesboro, TN, 37132, United States.
Austin WolvingtonDepartment of Chemistry, Middle Tennessee State University, 1301 East Main Street, Murfreesboro, TN, 37132, United States.
Catherine T NguyenDepartment of Chemistry and Biochemistry, Georgia Southern University, 11935 Abercorn Street, Savannah, GA, 31419, United States.
Laiba KhanDepartment of Chemistry and Biochemistry, Georgia Southern University, 11935 Abercorn Street, Savannah, GA, 31419, United States.
Claros CabreraMonacan High School, 11501 Smoketree Dr, Richmond, VA 23236, United States.
Mark Vincent C Dela CernaDepartment of Chemistry and Biochemistry, Georgia Southern University, 11935 Abercorn Street, Savannah, GA, 31419, United States.
Jamie R WallenWestern Carolina University, Department of Chemistry and Physics, 111 Memorial Drive, Cullowhee, NC 28723, United States.
Mitch H WeilandDepartment of Chemistry and Biochemistry, Georgia Southern University, 11935 Abercorn Street, Savannah, GA, 31419, United States.
Justin M MillerDepartment of Chemistry, Middle Tennessee State University, 1301 East Main Street, Murfreesboro, TN, 37132, United States.ORCID 0000-0002-4744-5192

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyaspartic acid (PAA) is a biodegradable polymer with various industrial applications. To date there are only three known PAA hydrolases (from the gene PahZ) capable of degrading PAA. These enzymes are expressed in two different bacteria, Sphingomonas sp. KT-1 (PahZ1KT-1 and PahZ2KT-1) and Pedobacter sp. KP-2 (PahZ1KP-2). PahZ1KT-1 and PahZ2KT-1 form a two-component system degrading tPAA to oligoaspartic acid (OAA) and subsequently into aspartic acid. This study aims to expand the diversity of PAA hydrolases and inform efforts to improve PAA degradation. To further understand the known PahZ1 homologs, the X-ray crystal structure of PahZ1KP-2 was determined to examine its structural homology with PahZ1KT-1. Crystallographic analysis revealed PahZ1KP-2 is monomeric, contrasting with the dimeric PahZ1KT-1, yet both share a conserved serine protease catalytic triad. With the aim of expanding the PahZ1 family, four putative homologs were identified using bioinformatics and AI-based structural modeling, all of which retained the α/β hydrolase domain. Importantly, all homologs exhibited measurable PAA-degrading activity and each was classified as either monomer or dimer to further expand the diversity of PahZ1 enzymes and provide a broader toolbox for sustainable polymer degradation.

Indexed as

Bacterial ProteinsHydrolasesPeptidesSphingomonasAmino Acid SequenceCrystallography, X-RayModels, MolecularBacterial ProteinsHydrolasesPeptidespolyaspartateenzymesPAA HydrolasesPoly(aspartic acid)Polymer HydrolaseProtein Homology

Identifiers

PMID41761765
PMCPMC13017698

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.