Hartig A, Ruis H
Eur J Biochem. 1986 Nov 3;160(3):487-90. doi: 10.1111/j.1432-1033.1986.tb10065.x.
A 2642-base-pair DNA fragment containing the catalase T (CTT1) structural gene of the yeast Saccharomyces cerevisiae and its flanking regions has been sequenced. The gene codes for a protein of 562 amino acids (relative molecular mass 64,449) and appears to contain no intron. The amino acid sequence of catalase T derived from the DNA sequence shows 40.7% homology (52.2% including conservative replacements) to that of bovine liver catalase. All amino acids previously postulated to participate directly in catalysis by liver catalase and most of the amino acids of the immediate environment of hemin, the prosthetic group of catalase, are conserved in catalase T. The data obtained indicate that the folding of polypeptide chains of the two catalases compared has been conserved within a central region consisting mainly of the beta-barrel domain, which bears the prosthetic group, and a major part of the "wrapping domain". N- and C-terminal regions involved in subunit interactions are less well conserved. It is suggested that their structure is more similar to that of the corresponding regions of Penicillium vitale catalase. However, catalase T lacks the C-terminal flavodoxin-like domain present in this protein.
已对一段包含酿酒酵母过氧化氢酶T（CTT1）结构基因及其侧翼区域的2642个碱基对的DNA片段进行了测序。该基因编码一种由562个氨基酸组成的蛋白质（相对分子质量为64449），且似乎不含内含子。从DNA序列推导得到的过氧化氢酶T的氨基酸序列与牛肝过氧化氢酶的氨基酸序列显示出40.7%的同源性（包括保守替换在内为52.2%）。所有先前假定直接参与肝脏过氧化氢酶催化作用的氨基酸以及过氧化氢酶辅基血红素紧邻区域的大多数氨基酸在过氧化氢酶T中都得以保留。所获得的数据表明，所比较的两种过氧化氢酶的多肽链折叠在一个主要由带有辅基的β桶结构域和“包裹结构域”的主要部分组成的中心区域内是保守的。参与亚基相互作用的N端和C端区域保守性较差。有人提出，它们的结构与活力青霉过氧化氢酶相应区域的结构更为相似。然而，过氧化氢酶T缺乏该蛋白质中存在的C端类黄素氧还蛋白结构域。
