The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate.
about
Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactionsBiotin and Lipoic Acid: Synthesis, Attachment, and Regulation.Protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism.The biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.Reconstitution of a thermostable xylan-degrading enzyme mixture from the bacterium Caldicellulosiruptor bescii.Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic Pathway.Product inhibition in the radical S-adenosylmethionine family.Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase.A biochemical sulfur delivery service.
P2860
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P2860
The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate.
description
2006 nî lūn-bûn
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
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2006年论文
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2006年论文
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name
The activity of a thermostable ...... synthetic octanoyl substrate.
@en
type
label
The activity of a thermostable ...... synthetic octanoyl substrate.
@en
prefLabel
The activity of a thermostable ...... synthetic octanoyl substrate.
@en
P2093
P356
P1476
The activity of a thermostable ...... synthetic octanoyl substrate.
@en
P2093
Marco Kriek
Penny Bryant
Robert J Wood
P356
10.1016/J.AB.2006.01.023
P407
P577
2006-02-03T00:00:00Z