Upshall A, Gilbert T, Saari G, O'Hara P J, Weglenski P, Berse B, Miller K, Timberlake W E
Mol Gen Genet. 1986 Aug;204(2):349-54. doi: 10.1007/BF00425521.
The transcriptional organization and sequence of the Aspergillus nidulans argB gene, encoding ornithine carbamoyl transferase (OCTase; E.C. 2.1.3.3.), was determined. Transcription of the gene begins within a methionine-initiated open translation reading frame, indicating that a second methionine codon of the open reading frame is used for translation initiation. The predicted length of the OCTase precursor peptide is 359 amino acids, and it contains a highly basic amino terminus that is probably involved in mitochondrial targeting. There is extensive homology between Aspergillus OCTase and mammalian and bacterial OCTases and weaker homology between the Aspergillus polypeptide and bacterial arginine carbamoyl transferase.
测定了构巢曲霉（Aspergillus nidulans）中编码鸟氨酸氨甲酰基转移酶（OCTase；E.C. 2.1.3.3）的argB基因的转录组织和序列。该基因的转录起始于一个由甲硫氨酸起始的开放翻译阅读框内，这表明开放阅读框中的第二个甲硫氨酸密码子被用于翻译起始。预测的OCTase前体肽长度为359个氨基酸，并且它含有一个高度碱性的氨基末端，这可能与线粒体靶向有关。构巢曲霉OCTase与哺乳动物和细菌的OCTase之间存在广泛的同源性，而构巢曲霉多肽与细菌精氨酸氨甲酰基转移酶之间的同源性较弱。
