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Structural Insight into the Reaction Mechanism of Ketosynth..:

Taichi Chisuga (6796307) ; Akira Nagai (11909912) ; Akimasa Miyanaga (1388373)...
https://figshare.com/articles/journal_contribution/Structural_Insight_into_the_Reaction_Mechanism_of_Ketosynthase-Like_Decarboxylase_in_a_Loading_Module_of_Modular_Polyketide_Synthases/17908511. , 2022

Link: https://doi.org/10.1021/acschembio.1c00856.s001

RT Journal
T1 <Title>Structural Insight into the Reaction Mechanism of Ketosynthase-Like Decarboxylase in a Loading Module of Modular Polyketide Synthases</Title>

UL https://suche.suub.uni-bremen.de/peid=base-ftsmithonian:oai:figshare.com:article_17908511&Exemplar=1&LAN=DE
				
A1 Taichi Chisuga (6796307)
A1 Akira Nagai (11909912)
A1 Akimasa Miyanaga (1388373)
A1 Ena Goto (5391788)
A1 Kosuke Kishikawa (11909915)
A1 Fumitaka Kudo (1388382)
A1 Tadashi Eguchi (1388379)
YR 2022
K1 Biophysics
K1 Biochemistry
K1 Medicine
K1 Genetics
K1 Evolutionary Biology
K1 Developmental Biology
K1 Inorganic Chemistry
K1 Virology
K1 Computational Biology
K1 Chemical Sciences not elsewhere classified
K1 present biochemical analyses
K1 high sequence similarity
K1 catalytic cys residue
K1 acylated cys residue
K1 pks starter unit
K1 enolate upon decarboxylation
K1 modular polyketide synthases
K1 fatty acid biosynthesis
K1 decarboxylation reaction catalyzed
K1 q </ sub
K1 ks domains suggests
K1 decarboxylation reaction
K1 vitro </
K1 methylmalonyl unit
K1 initiates decarboxylation
K1 gln residue
K1 widely distributed
K1 suitable conformation
K1 structural insight
K1 mutational analysis
K1 methylmalonyl units
K1 loading modules
K1 loading module
K1 like decarboxylase
K1 ks domains
K1 gfsa ks
K1 enabled identification
K1 domain mimics
K1 decarboxylative condensation
K1 cmip4 ks
K1 analysis showed
K1 active site
JF https://figshare.com/articles/journal_contribution/Structural_Insight_into_the_Reaction_Mechanism_of_Ketosynthase-Like_Decarboxylase_in_a_Loading_Module_of_Modular_Polyketide_Synthases/17908511
LK http://dx.doi.org/https://doi.org/10.1021/acschembio.1c00856.s001
DO https://doi.org/10.1021/acschembio.1c00856.s001
SF ELIB - SuUB Bremen

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