Isobe K, Nokihara K
Enzyme Technology and Natural Products Chemistry Division, GBF-Gesellschaft für Biotechnologische Forschung mbH, Braunschweig, Germany.
FEBS Lett. 1993 Apr 5;320(2):101-6. doi: 10.1016/0014-5793(93)80071-2.
The complete amino acid sequence of mono- and diacylglycerol lipase from Penicillium camembertii was determined. This lipase has a single polypeptide chain consisting of 276 amino acid residues with two disulfide linkages. The primary structure was revealed by sequencing the digests of the intact and S-pyridylethylated proteins by trypsin, endoproteinase Lys-C and V8 protease. The two-dimensional electrophoresis was also carried out to confirm the internal sequence. The catalytic triad of this lipase was Ser, Asp and His, and one potential N-glycosylation site was also revealed.
测定了来自卡门柏青霉的单酰甘油脂肪酶和二酰甘油脂肪酶的完整氨基酸序列。这种脂肪酶有一条由276个氨基酸残基组成的单多肽链，带有两个二硫键。通过对完整蛋白和S-吡啶基乙基化蛋白用胰蛋白酶、内肽酶Lys-C和V8蛋白酶进行消化测序，揭示了其一级结构。还进行了二维电泳以确认内部序列。该脂肪酶的催化三联体为丝氨酸、天冬氨酸和组氨酸，同时还揭示了一个潜在的N-糖基化位点。
