Partial characterization of the gene encoding myoadenylate deaminase from the teleost fish Platichthys flesus.
AMP-deaminase (AMPD, EC 3.5.4.6), which catalyzes the irreversible hydrolytic deamination of AMP to IMP and ammonia, is an important energy-related enzyme. The partial genomic sequence of the gene encoding myoadenylate deaminase (AMPD1) from the teleost fish Platichthys flesus was determined. The amino acid sequence of P. flesus AMPD1 shows 82% homology with that of the teleost fish Danio rerio. Comparison of genomic sequences of P. flesus and Rattus norvegicus reveals a high degree of conservation of both sequence and structural organization. A phylogenetic analysis of AMPD sequences shows that bony fish and mammalian AMPD1s arise by duplication of a common primordial gene.
Thébault
M T
MT
UMR CNRS 6539, Laboratoire des Sciences de l'Environnement Marin, Institut Universitaire Européen de la Mer, Université de Brest, Place Nicolas Copernic, 29280, Plouzané, France. marie-therese.thebault@univ-brest.fr
Tanguy
A
A
Meistertzheim
A L
AL
Raffin
J P
JP
D000659:AMP Deaminase / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D016000:Cluster Analysis; D017124:Conserved Sequence / Q000235:genetics; D017931:DNA Primers / Q000235:genetics; D005412:Flatfishes / Q000235:genetics*; D040461:Gene Components; D020131:Genes, Duplicate / Q000235:genetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D051381:Rats; D017422:Sequence Analysis, DNA
D017931:DNA Primers; D000659:AMP Deaminase