Efficient tryptophan-catabolizing activity is consistently conserved through evolution of TDO enzymes, but not IDO enzymes.
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Sea lampreys elicit strong transcriptomic responses in the lake trout liver during parasitismIdentification of an evolutionary conserved structural loop that is required for the enzymatic and biological function of tryptophan 2,3-dioxygenase.Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable.High l-Trp affinity of indoleamine 2,3-dioxygenase 1 is attributed to two residues located in the distal heme pocket.
P2860
Efficient tryptophan-catabolizing activity is consistently conserved through evolution of TDO enzymes, but not IDO enzymes.
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2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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name
Efficient tryptophan-cataboliz ...... enzymes, but not IDO enzymes.
@en
type
label
Efficient tryptophan-cataboliz ...... enzymes, but not IDO enzymes.
@en
prefLabel
Efficient tryptophan-cataboliz ...... enzymes, but not IDO enzymes.
@en
P2860
P356
P1476
Efficient tryptophan-cataboliz ...... enzymes, but not IDO enzymes.
@en
P2093
Hajime J Yuasa
P2860
P304
P356
10.1002/JEZ.B.22608
P50
P577
2015-02-20T00:00:00Z