A polyamine-independent role for

Adenosylmethionine Decarboxylase / chemistry Arabidopsis / enzymology Arabidopsis Proteins / chemistry Putrescine / chemistry Ralstonia pickettii / enzymology Saccharomyces cerevisiae / enzymology Saccharomyces cerevisiae Proteins / chemistry Shewanella / enzymology Spermidine / chemistry
biosynthesis enzyme activity evolutionary biology genomics metabolism polyamines

Journal

The Biochemical journal
ISSN: 1470-8728
Titre abrégé: Biochem J
Pays: England
ID NLM: 2984726R

Informations de publication

Date de publication:
20 09 2019
Historique:
received: 05 08 2019
revised: 27 08 2019
accepted: 29 08 2019
pubmed: 31 8 2019
medline: 19 3 2020
entrez: 31 8 2019
Statut: epublish

Résumé

The only known function of

Identifiants

DOI: 10.1042/BCJ20190561 PMID: 31467246
pubmed: 31467246
pii: BCJ20190561
doi: 10.1042/BCJ20190561
doi:

Substances chimiques

Arabidopsis Proteins 0
Saccharomyces cerevisiae Proteins 0
Adenosylmethionine Decarboxylase EC 4.1.1.50
Spermidine U87FK77H25
Putrescine V10TVZ52E4

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2579-2594

Informations de copyright

© 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.

Auteurs

Bin Li (B)

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A.

Shin Kurihara (S)

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A.

Sok Ho Kim (SH)

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A.

Jue Liang (J)

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A.

Anthony J Michael (AJ)

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, U.S.A anthony.michael@utsouthwestern.edu.
ORCID: 0000-0003-2956-9148

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Classifications MeSH

questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Lyases › Carbon-carbon lyases › Carboxy-lyases › Adenosylmethionine decarboxylase › A polyamine-independent role for
questionsmedicales.fr › Eucaryotes › Viridiplantae › Streptophyta › Embryophyta › Tracheobionta › Magnoliopsida › Brassicaceae › Arabidopsis › A polyamine-independent role for
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines végétales › Protéines d'Arabidopsis › A polyamine-independent role for
questionsmedicales.fr › Composés chimiques organiques › Amines › Polyamines › Diamines › Putrescine › A polyamine-independent role for
questionsmedicales.fr › Bactéries › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia › Ralstonia pickettii › A polyamine-independent role for
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › A polyamine-independent role for
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › A polyamine-independent role for
questionsmedicales.fr › Bactéries › Proteobacteria › Gammaproteobacteria › Alteromonadaceae › Shewanella › A polyamine-independent role for
questionsmedicales.fr › Composés chimiques organiques › Amines › Polyamines › Spermidine › A polyamine-independent role for