Protein sequences of arylsulfatases, phosphonate monoester hydrolases, and reconstructed ancestors (ICPSR doi:10.18419/darus-1801)

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Part 2: Study Description
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Document Description

Citation

Title:

Protein sequences of arylsulfatases, phosphonate monoester hydrolases, and reconstructed ancestors

Identification Number:

doi:10.18419/darus-1801

Distributor:

DaRUS

Date of Distribution:

2021-05-03

Version:

1

Bibliographic Citation:

Heberlein, Magdalena, 2021, "Protein sequences of arylsulfatases, phosphonate monoester hydrolases, and reconstructed ancestors", https://doi.org/10.18419/darus-1801, DaRUS, V1

Study Description

Citation

Title:

Protein sequences of arylsulfatases, phosphonate monoester hydrolases, and reconstructed ancestors

Identification Number:

doi:10.18419/darus-1801

Authoring Entity:

Heberlein, Magdalena

Distributor:

DaRUS

Access Authority:

Pleiss, Jürgen

Depositor:

Buchholz, Patrick C. F.

Date of Deposit:

2021-04-15

Study Scope

Keywords:

Medicine, Health and Life Sciences, amino acid sequence, protein sequence, ancestor reconstruction, phylogeny

Abstract:

Protein sequences were derived from a maximum-likelihood phylogenetic tree for arylsulfatases and phosphonate monoester hydrolases, including a selection of reconstructed ancestral sequences.

Notes:

This dataset comprises 95 protein sequences annotated as homologues of arylsulfatases (AS) and 85 protein sequences annotated as homologues of phosphonate monoester hydrolases (PMH). In addition to these 180 protein sequences, 58 ancestral protein sequences were reconstructed from a maximum-likelihood phylogenetic tree ("node_").

Methodology and Processing

Sources Statement

Data Sources:

van Loo B, Schober M, Valkov E, Heberlein M, Bornberg-Bauer E, Faber K, et al. "Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester." J Mol Biol. 2018;430: 1004-1023. <a href="https://doi.org/10.1016/j.jmb.2018.02.010">doi:10.1016/j.jmb.2018.02.010</a>

van Loo B, Bayer CD, Fischer G, Jonas S, Valkov E, Mohamed MF, et al. "Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily." J Am Chem Soc. 2019;141: 370-387. <a href="https://doi.org/10.1021/jacs.8b10290">doi:10.1021/jacs.8b10290</a>

Heberlein M: "Evolution of substrate specificity in the alkaline phosphatase superfamily". Dissertation, Westfälische Wilhelms-Universität Münster, Germany, 2016 <a href="https://stg.ibs-bw.de/aDISWeb/app?service=direct/0/Home/$DirectLink&sp=SOPAC02&sp=SAKSWB-IdNr155480020X">https://stg.ibs-bw.de/aDISWeb/app?service=direct/0/Home/$DirectLink&sp=SOPAC02&sp=SAKSWB-IdNr155480020X</a>

Data Access

Notes:

CC BY Waiver

Other Study Description Materials

Related Studies

<a href="https://doi.org/10.18419/darus-817">https://doi.org/10.18419/darus-817</a>

Related Publications

Citation

Bibliographic Citation:

Patrick C. F. Buchholz, Bert van Loo, Bernard D. G. Eenink, Erich Bornberg-Bauer, Jürgen Pleiss: "Ancestral sequences of a large promiscuous enzyme family correspond to bridges in sequence space in a network representation" (submitted)

Other Study-Related Materials

Label:

AS_PMH_ancestors.fasta

Text:

FASTA file for 238 protein sequences

Notes:

application/octet-stream