2016
DOI: 10.1016/j.plaphy.2016.05.031
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Cloning and biochemical characterization of indole-3-acetic acid-amino acid synthetase PsGH3 from pea

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Cited by 9 publications
(5 citation statements)
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“…The proteins encoded by these genes are 92% identical, and the plasmid-located copy has been expressed heterologously and functionally characterized [ 37 ]. IAAL is postulated to convert free IAA into less active conjugated forms [ 38 ]. Heterologous expression of IAAL in tobacco and potato led to abnormal developmental changes [ 39 ].…”
Section: Resultsmentioning
confidence: 99%
“…The proteins encoded by these genes are 92% identical, and the plasmid-located copy has been expressed heterologously and functionally characterized [ 37 ]. IAAL is postulated to convert free IAA into less active conjugated forms [ 38 ]. Heterologous expression of IAAL in tobacco and potato led to abnormal developmental changes [ 39 ].…”
Section: Resultsmentioning
confidence: 99%
“…The proteins encoded by these genes are 92% identical, and the plasmid-located copy has been expressed heterologously and functionally characterized [37]. IAAL is postulated to convert free IAA into less active conjugate forms [38]. Heterologous expression of IAAL in tobacco and potato led to abnormal developmental changes [39].…”
Section: Resultsmentioning
confidence: 99%
“…The likely reason for that is differences in the kinetics of the enzymatic reactions of auxin biosynthesis and metabolisation. There is some evidence that Yucca flavin-dependent monooxygenases, which catalyse the rate-limiting step in IAA synthesis, have slow kinetics [ 110 , 111 ], whereas IAA–amino synthases encoded by genes of the family GH3 are described as enzymes with fast kinetics [ 80 , 112 , 113 , 114 ].…”
Section: Discussionmentioning
confidence: 99%