Evidence map›Paper›PMID 27452902›Full record

ArticleProtein science : a publication of the Protein Society2016

The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent.

Yi Lin, Cody J Boese, Martin St Maurice

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 26% of its field
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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026
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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

3 authors at 1 institution in 1 country.

Yi LinDepartment of Biological Sciences, Marquette University, Milwaukee, Wisconsin, 53201.
Cody J BoeseDepartment of Biological Sciences, Marquette University, Milwaukee, Wisconsin, 53201.
Martin St MauriceDepartment of Biological Sciences, Marquette University, Milwaukee, Wisconsin, 53201. martin.stmaurice@marquette.edu.
Marquette University · US

Funding

Investigation of the structure and function of urea amidolyaseR15GM097724 · NIGMS · MARQUETTE UNIVERSITY · PI ST. MAURICE, MARTIN RAOUL · 2012 to 2012
$346k
NIGMS NIH HHS R15 GM097724
6 · The paper itself

Abstract

Urea amidolyase (UAL) is a multifunctional biotin-dependent enzyme that contributes to both bacterial and fungal pathogenicity by catalyzing the ATP-dependent cleavage of urea into ammonia and CO2 . UAL is comprised of two enzymatic components: urea carboxylase (UC) and allophanate hydrolase (AH). These enzyme activities are encoded on separate but proximally related genes in prokaryotes while, in most fungi, they are encoded by a single gene that produces a fusion enzyme on a single polypeptide chain. It is unclear whether the UC and AH activities are connected through substrate channeling or other forms of direct communication. Here, we use multiple biochemical approaches to demonstrate that there is no substrate channeling or interdomain/intersubunit communication between UC and AH. Neither stable nor transient interactions can be detected between prokaryotic UC and AH and the catalytic efficiencies of UC and AH are independent of one another. Furthermore, an artificial fusion of UC and AH does not significantly alter the AH enzyme activity or catalytic efficiency. These results support the surprising functional independence of AH from UC in both the prokaryotic and fungal UAL enzymes and serve as an important reminder that the evolution of multifunctional enzymes through gene fusion events does not always correlate with enhanced catalytic function.

Indexed as

Allophanate HydrolaseBacterial ProteinsCarbon-Nitrogen LigasesCatalysisPseudomonas syringaeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAllophanate HydrolaseBacterial ProteinsCarbon-Nitrogen LigasesSaccharomyces cerevisiae Proteinsurea carboxylase (hydrolyzing)biotinenzymeevolutionmultidomainmultifunctionalsubstrate channeling

Identifiers

PMID27452902
PMCPMC5029531
OpenAlexW2476532643

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.