Activity of α-Aminoadipate Reductase Depends on the N-Terminally Extending Domain.
about
Structural insight into the necessary conformational changes of modular nonribosomal peptide synthetases.A non-canonical peptide synthetase adenylates 3-methyl-2-oxovaleric acid for auriculamide biosynthesis.An Activator of an Adenylation Domain Revealed by Activity but Not Sequence Homology.Prerequisites of Isopeptide Bond Formation in Microcystin Biosynthesis.
P2860
Activity of α-Aminoadipate Reductase Depends on the N-Terminally Extending Domain.
description
2015 nî lūn-bûn
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2015年の論文
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name
Activity of α-Aminoadipate Reductase Depends on the N-Terminally Extending Domain.
@en
type
label
Activity of α-Aminoadipate Reductase Depends on the N-Terminally Extending Domain.
@en
prefLabel
Activity of α-Aminoadipate Reductase Depends on the N-Terminally Extending Domain.
@en
P2093
P2860
P356
P1433
P1476
Activity of α-Aminoadipate Reductase Depends on the N-Terminally Extending Domain.
@en
P2093
Daniel Kalb
Dirk Hoffmeister
Gerald Lackner
Marcus Rappe
P2860
P304
P356
10.1002/CBIC.201500190
P577
2015-06-11T00:00:00Z