From: Charles Plessy Date: Mon, 2 Jul 2018 05:58:16 +0000 (+0900) Subject: Ein prosit. X-Git-Url: https://source.charles.plessy.org/?a=commitdiff_plain;h=ae43f83ac660509fc01511df9e37d91c46aa5211;p=source%2F.git Ein prosit. --- diff --git a/biblio/20141418.mdwn b/biblio/20141418.mdwn new file mode 100644 index 00000000..c2f2dba2 --- /dev/null +++ b/biblio/20141418.mdwn @@ -0,0 +1,10 @@ +[[!meta title="Oikopleura dioica alcohol dehydrogenase class 3 provides new insights into the evolution of retinoic acid synthesis in chordates."]] +[[!tag Oikopleura metabolism]] + +Zoolog Sci. 2010 Feb;27(2):128-33. doi:10.2108/zsj.27.128. + +Oikopleura dioica alcohol dehydrogenase class 3 provides new insights into the evolution of retinoic acid synthesis in chordates. + +Cañestro C, Albalat R, Postlethwait JH. + +[[!pmid 20141418 desc="Adh3 is the only MDR-Adh in the _Oikopleura_ genome. It strictly conserves the eight residues that constitute the signature of all Adh3 and other residues as well, therefore probably metabolising the same types of substrates as in other species. (Adh3 is the ancestral MDR-Adh genes in vertebrates; Adh1, 2 and 4 show signs of neofunctionalisation)."]] diff --git a/tags/Oikopleura.mdwn b/tags/Oikopleura.mdwn index 1466f8a2..b9deb058 100644 --- a/tags/Oikopleura.mdwn +++ b/tags/Oikopleura.mdwn @@ -133,7 +133,9 @@ Physiology - Searching for an immune system, [[Denoeud et al., 2010|biblio/21097902]] excluded LRR proteins, as none of the 74 models found had a transmembrane domain. - + - Adh3 is the only medium-chain alcohol dehydrogenase (MDR-Adh) in _Oikopleura_ + (like in other non-vertebrates). Conservation of critical residues and similarity + in expression pattern suggest that its metabolic targets are the same as in other species. Phenotypes ----------