Lattion A L, Soubrier F, Allegrini J, Hubert C, Corvol P, Alhenc-Gelas F
INSERM U36, Paris, France.
FEBS Lett. 1989 Jul 31;252(1-2):99-104. doi: 10.1016/0014-5793(89)80897-x.
The endothelial angiotensin I-converting enzyme (ACE) is organized in two large homologous domains, each bearing a putative active site. However, only one of these sites is probably involved in catalyzing the conversion of angiotensin I into angiotensin II. The testicular form of ACE is equally active, encoded by the same gene, but translated from a shorter mRNA. Molecular cloning of the human testicular ACE cDNA indicates that the mRNA codes for 732 residues (vs 1306 in endothelium). The testicular transcript corresponds to the 3' half of the endothelial transcript and encodes one of the two homologous domains of endothelial ACE, preceded by a short specific sequence. This 5' specific sequence contains 228 nucleotides and encodes 67 amino acids, including the putative signal peptide followed by a serine/threonine-enriched region, presumably glycosylated. The testicular transcript corresponds to the ancestral, non-duplicated form of the ACE gene. Since the carboxyl-terminal domain of the endothelial ACE is expressed in the testicular enzyme, it is likely that it bears the active site in both forms.
内皮血管紧张素I转换酶（ACE）由两个大的同源结构域组成，每个结构域都有一个假定的活性位点。然而，这些位点中可能只有一个参与催化血管紧张素I转化为血管紧张素II。睾丸形式的ACE同样具有活性，由相同的基因编码，但由较短的mRNA翻译而来。人睾丸ACE cDNA的分子克隆表明，该mRNA编码732个残基（内皮中为1306个）。睾丸转录本对应于内皮转录本的3' 半部分，并编码内皮ACE两个同源结构域之一，前面有一个短的特定序列。这个5' 特定序列包含228个核苷酸，编码67个氨基酸，包括假定的信号肽，后面是一个富含丝氨酸/苏氨酸的区域，可能是糖基化的。睾丸转录本对应于ACE基因的原始、未重复形式。由于内皮ACE的羧基末端结构域在睾丸酶中表达，两种形式的活性位点可能都位于该结构域。
