Sabina R L, Marquetant R, Desai N M, Kaletha K, Holmes E W
J Biol Chem. 1987 Sep 15;262(26):12397-400.
Myoadenylate deaminase is the muscle-specific isoform of AMP deaminase (EC 3.5.4.6), an enzyme which plays a special role in energy metabolism in skeletal muscle. A 2.3-kilobase cDNA encoding this enzyme has been cloned from a lambda gt10 library prepared from rat skeletal muscle using oligonucleotide probes designed from AMP deaminase peptide sequences. This cDNA was sequenced, and the amino acid sequence of this isoform of AMP deaminase was deduced. Sequences homologous to this cDNA are identified in the genome of eukaryotes as diverse as yeast and man. Tissue-specific expression of a 2.5-kilobase AMP deaminase transcript is demonstrated, and the abundance of this transcript as well as the 80-kDa adult, muscle-specific peptide of AMP deaminase increase in parallel during postnatal skeletal muscle development. In the adult animal, the abundance of this transcript and AMP deaminase activity are differentially expressed in various skeletal muscle fiber types. We conclude that AMP deaminase sequences have been highly conserved during evolution, and in mammals there is developmental and tissue-specific control of expression of this gene.
肌腺苷酸脱氨酶是AMP脱氨酶（EC 3.5.4.6）的肌肉特异性同工型，该酶在骨骼肌的能量代谢中起特殊作用。利用从AMP脱氨酶肽序列设计的寡核苷酸探针，已从大鼠骨骼肌制备的λgt10文库中克隆出编码该酶的2.3千碱基cDNA。对该cDNA进行了测序，并推导了这种AMP脱氨酶同工型的氨基酸序列。在从酵母到人类等多种真核生物的基因组中都鉴定出了与该cDNA同源的序列。证实了2.5千碱基AMP脱氨酶转录本的组织特异性表达，并且在出生后骨骼肌发育过程中，该转录本的丰度以及80 kDa的成年肌肉特异性AMP脱氨酶肽平行增加。在成年动物中，该转录本的丰度和AMP脱氨酶活性在各种骨骼肌纤维类型中差异表达。我们得出结论，AMP脱氨酶序列在进化过程中高度保守，并且在哺乳动物中，该基因的表达存在发育和组织特异性调控。
