Expression, purification and crystallization of N-acetyl-(R)-β-phenylalanine acylases derived from Burkholderia sp. AJ110349 and Variovorax sp. AJ110348 and structure determination of the Burkholderia enzyme.

Yuki Kato, Hisashi Kawasaki, Tsuyoshi Nakamatsu, Namio Matsuda, Ryo Natsume

Open access · greenAbstract read

In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.1field-weighted citation impact, top 69% 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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 1 citations in OpenAlex.

Role of Active Site Residues and Weak Noncovalent Interactions in Substrate Positioning inBiochemistry · 2025
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4 · The record

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5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Yuki KatoGraduate School of Advanced Science and Technology, Tokyo Denki University, 5 Senju-asahi-cho, Adachi-ku, Tokyo 120-8551, Japan.

Hisashi KawasakiGraduate School of Advanced Science and Technology, Tokyo Denki University, 5 Senju-asahi-cho, Adachi-ku, Tokyo 120-8551, Japan.

Tsuyoshi NakamatsuGraduate School of Advanced Science and Technology, Tokyo Denki University, 5 Senju-asahi-cho, Adachi-ku, Tokyo 120-8551, Japan.

Namio MatsudaGraduate School of Advanced Science and Technology, Tokyo Denki University, 5 Senju-asahi-cho, Adachi-ku, Tokyo 120-8551, Japan.

Ryo NatsumeGraduate School of Advanced Science and Technology, Tokyo Denki University, 5 Senju-asahi-cho, Adachi-ku, Tokyo 120-8551, Japan.

Tokyo Denki University · JP

Funding

Japan Society for the Promotion of Science 15K07401Tokyo Denki University Q13L-01

6 · The paper itself

Abstract

N-Acetyl-(R)-β-phenylalanine acylase is an enzyme that hydrolyzes the amide bond of N-acetyl-(R)-β-phenylalanine to produce enantiopure (R)-β-phenylalanine. In previous studies, Burkholderia sp. AJ110349 and Variovorax sp. AJ110348 were isolated as (R)-enantiomer-specific N-acetyl-(R)-β-phenylalanine acylase-producing organisms and the properties of the native enzyme from Burkholderia sp. AJ110349 were characterized. In this study, structural analyses were carried out in order to investigate the structure-function relationships of the enzymes derived from both organisms. The recombinant N-acetyl-(R)-β-phenylalanine acylases were crystallized by the hanging-drop vapor-diffusion method under multiple crystallization solution conditions. The crystals of the Burkholderia enzyme belonged to space group P4

Indexed as

BurkholderiaAmidohydrolasesCrystallizationCrystallography, X-RayPhenylalanineamidaseAmidohydrolasesPhenylalanineBurkholderia sp. AJ110349enantiomer-specific amidohydrolysisN-acetyl-(R)-β-phenylalanine acylaseVariovorax sp. AJ110348β-phenylalanine

Identifiers

PMID36862095

DOI10.1107/S2053230X23000730

PMCPMC9979978

OpenAlexW4321616069

What OpenQuestion holds

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Registered trials

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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.