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首页> 外文期刊>Journal of biochemical and molecular toxicology >Liver prenylated methylated protein methyl esterase is the same enzyme as Sus scrofa carboxylesterase.
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Liver prenylated methylated protein methyl esterase is the same enzyme as Sus scrofa carboxylesterase.

机译：肝脏戊烯基化甲基化蛋白质甲基酯酶与Sus scrofa羧酸酯酶相同。

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摘要

The C-terminal --COOH of prenylated proteins is methylated to --COOCH3. The --COOCH3 ester forms are hydrolyzed by prenylated methylated protein methyl esterase (PMPMEase) to the original acid forms. This is the only reversible step of the prenylation pathway. PMPMEase has not been purified and identified and is therefore understudied. Using a prenylated-L-cysteine methyl ester as substrate, PMPMEase was purified to apparent homogeneity from porcine liver supernatant. SDS-PAGE analysis revealed an apparent mass of 57 kDa. Proteomics analyses identified 17 peptides (242 amino acids). A Mascot database search revealed these as portions of the Sus scrofa carboxylesterase, a 62-kDa serine hydrolase with the C-terminal HAEL endoplasmic reticulum-retention signal. It is at least 71% identical to such mammalian carboxylesterases as human carboxylesterase 1 with affinities toward hydrophobic substrates and known to activate prodrugs, metabolize active drugs, as well as detoxify various substances such as cocaine and food-derived esters. The purified enzyme hydrolyzed benzoyl-Gly-farnesyl-L-cysteine methyl ester and hydrocinamoyl farnesyl-L-cysteine methyl ester with Michaelis-Menten constant (K(m)) values of 33 +/- 4 and 25 +/- 4 microM and V(max) values of 4.51 +/- 0.28 and 6.80 +/- 0.51 nmol/min/mg of protein, respectively. It was inhibited by organophosphates, chloromethyl ketones, ebelactone A and B, and phenylmethylsulfonyl fluoride.
机译：烯丙基化蛋白质的C末端--COOH被甲基化为--COOCH3。 --COOCH3酯的形式通过烯丙基化的甲基化蛋白质甲基酯酶（PMPMEase）水解成原始的酸形式。这是异戊二烯化途径的唯一可逆步骤。 PMPMEase尚未纯化和鉴定，因此尚未得到研究。使用烯丙基化的L-半胱氨酸甲酯作为底物，从猪肝上清液中纯化PMPMEase使其具有明显的同质性。 SDS-PAGE分析显示表观质量为57kDa。蛋白质组学分析鉴定出17种肽（242个氨基酸）。 Mascot数据库搜索显示这些是Sus scrofa羧酸酯酶的一部分，这是一种具有C末端HAEL内质网保留信号的62 kDa丝氨酸水解酶。它与诸如人羧酸酯酶1的哺乳动物羧酸酯酶具有至少71％的相同性，并且对疏水性底物具有亲和力，并且已知能激活前药，代谢活性药物以及对各种物质（例如可卡因和食物衍生的酯）进行解毒。纯化的酶水解了Michaelis-Menten常数（K（m））值为33 +/- 4和25 +/- 4 microM的苯甲酰基-甘氨酸-法呢尼基-L-半胱氨酸甲酯和氢肉桂酰基法呢基-L-半胱氨酸甲酯和蛋白质的V（max）值分别为4.51 +/- 0.28和6.80 +/- 0.51 nmol / min / mg。它被有机磷酸盐，氯甲基酮，依贝内酯A和B和苯甲基磺酰氟抑制。

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