Evidence map›Paper›PMID 21369990›Full record

ArticleJournal of microbiology (Seoul, Korea)2011

Purification and characterization of a new L-methioninase from solid cultures of Aspergillus flavipes.

Ashraf S A El-Sayed

Abstract read
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Article in Journal of microbiology (Seoul, Korea), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 73 citations in OpenAlex.

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  14. Biochemical Properties of Tyrosinase fromMolecules (Basel, Switzerland) · 2021
    Article
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  17. Review
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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

1 author at 1 institution in 1 country.

Ashraf S A El-SayedMicrobiology Department, Faculty of Science, Zagazig University, Zagazig, 44519, Egypt. ash_elsayed25@yahoo.com
Zagazig University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-Methioninase was purified to electrophoretic homogeneity from cultures of Aspergillus flavipes using anion-exchange and gel filtration chromatography by 12.1 fold compared to the crude enzyme preparation. The purified enzyme had a molecular mass of 47 kDa under denaturing conditions and an isoelectric point of 5.8 with no structural glycosyl residues. The enzyme had optimum activity at pH 7.8 and pH stability from 6.8-8.0 at 35°C. The enzyme appeared to be catalytically stable below 40°C. The enzyme activity was strongly inhibited by DL-propargylglycine, hydroxylamine, PMSF, 2-mercaptoethanol, Hg(+), Cu(2+), and Fe(2+), with slight inhibition by Triton X-(100). A flavipes L-methioninase has a higher catalytic affinity towards L-methionine (Km, 6.5 mM and Kcat, 14.1 S(-1)) followed by a relative demethiolating activity to L-homo-cysteine (Km, 12 mM and Kcat, 9.3 S(-1)). The enzyme has two absorption maxima at 280 and 420 nm, typical of other PLP-enzymes. Apo-L-methioninase has the ability to reconstitute its structural catalytic state completely upon addition of 0.15 mM PLP. L-Methioninase has neither an appreciable effect on liver function, platelet aggregation, nor hemolysis of human blood. The purified L-methioninase from solid cultures of A. flavipes displayed unique biochemical and catalytic properties over the currently applied Pseudomonad enzyme.

Indexed as

AnimalsAspergillusCarbon-Sulfur LyasesCell AggregationChromatography, GelChromatography, Ion ExchangeEnzyme InhibitorsEnzyme StabilityHemolysisHomocysteineHumansHydrogen-Ion ConcentrationIsoelectric PointKineticsLiver Function TestsMethionineCarbon-Sulfur LyasesEnzyme InhibitorsHomocysteineL-methionine gamma-lyaseMethionine

Identifiers

PMID21369990
OpenAlexW2072888427

What OpenQuestion holds

Textmetadata
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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.