Expression and Partial Purification of a Recombinant Secretory Form of Human Liver Carboxylesterase

Miller, Amanda; Scott, David F.; Chacko, Terry L.; Maxwell, Donald M.; Schlager, John J.; Lanclos, Kenneth D.

doi:10.1006/prep.1999.1121

Cited by 12 publications

(4 citation statements)

References 38 publications

(40 reference statements)

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“…CES1 HIEL and CES2 HTEL C-terminal sequences, and similar tetrapeptide sequences, have been previously shown to direct the microlocalization of mammalian liver CES within the endoplasmic reticulum (Robbi and Beaufay, 1991). Miller and coworkers (1999) have modified this sequence for human CES1 using site-directed mutagenesis to that of HIER, substituting the C-terminal leucine with arginine, and observed that the enzyme was secreted rather than retained within the cultured cells examined. Human and other mammalian CES5 sequences normally have a long hydrophobic C-terminal sequence which apparently provides the trigger for secretion.…”

Section: Ces5 Functional Aspectsmentioning

confidence: 99%

Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Holmes

Cox

VandeBerg

2008

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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Carboxylesterase 5 (CES5) (also called cauxin or CES7) is one of at least five mammalian CES gene families encoding enzymes of broad substrate specificity and catalysing hydrolytic and transesterification reactions. In silico methods were used to predict the amino acid sequences, secondary structures and gene locations for CES5 genes and gene products. Amino acid sequence alignments of mammalian CES5 enzymes enabled identification of key CES sequences previously reported for human CES1, as well as other sequences that are specific to the CES5 gene family, which were consistent with being monomeric in subunit structure and available for secretion into body fluids. Predicted secondary structures for mammalian CES5 demonstrated significant conservation with human CES1 as well as distinctive mammalian CES5 like structures. Mammalian CES5 genes are located in tandem with the CES1 gene(s), are transcribed on the reverse strand and contained 13 exons. CES5 has been previously reported in high concentrations in the urine (cauxin) of adult male cats, and within a protein complex of mammalian male epididymal fluids. Roles for CES5 may include regulating urinary levels of male cat pheromones; catalysing lipid transfer reactions within mammalian male reproductive fluids; and protecting neural tissue from drugs and xenobiotics.

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Section: Ces5 Functional Aspectsmentioning

confidence: 99%

Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Holmes

Cox

VandeBerg

2008

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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“…Some carboxylesterases from animals, plants, and insects have been purified, characterized and used to degrade malathion (Miller et al 1999; Yoshii et al 2007b; Cao et al 2008). Several malathion-degrading strains have been isolated, and degradation studies have also been carried out (Foster and Bia 2004; Hashmi et al 2004; Goda et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression and characterization of a malathion-hydrolyzing carboxylesterase from a thermophilic bacterium, Alicyclobacillus tengchongensis

Xie

Ding

et al. 2013

Biotechnol Lett

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A carboxylesterase gene from thermophilic bacterium, Alicyclobacillus tengchongensis, was cloned and expressed in Escherichia coli BL21 (DE3). The gene coded for a 513 amino acid protein with a calculated molecular mass of 57.82 kDa. The deduced amino acid sequence had structural features highly conserved among serine hydrolases, including Ser204, Glu325, and His415 as a catalytic triad, as well as type-B carboxylesterase serine active site (FGGDPENITIGGQSAG) and type-B carboxylesterase signature 2 (EDCLYLNIWTP). The purified enzyme exhibited optimum activity with β-naphthyl acetate at 60 °C and pH 7 as well as stability at 25 °C and pH 7. One unit of the enzyme hydrolyzed 5 mg malathion l−1 by 50 % within 25 min and 89 % within 100 min. The enzyme strongly degraded malathion and has a potential use for the detoxification of malathion residues.

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“…The bovine CES1.2A C-terminus lacks this sequence however which may alter the distribution characteristics for this enzyme. Miller and coworkers (1999) have described a bioengineered form of human CES1 for which the His-Ile-Glu-Leu was changed with a replacement Arginine at the C-terminus. This resulted in the secretion of this enzyme from human 293T cells in comparison with the native enzyme which was retained within the endoplasmic reticulum.…”

Section: Discussionmentioning

confidence: 99%

Bovine carboxylesterases: Evidence for two CES1 and five families of CES genes on chromosome 18

Holmes

Cox

VandeBerg

2009

Comparative Biochemistry and Physiology Part D: Genomics and Pr

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Predicted bovine carboxylesterase (CES) protein and gene sequences were derived from bovine (Bos taurus) genomic sequence data. Two bovine CES1 genes (CES1.1 and CES1.2) were located on chromosome 18 encoding amino acid sequences that were 81% identical. Two forms of CES1.2 were also observed apparently caused by an indel polymorphism encoded at the C-terminus end. Two CES gene clusters were observed on chromosome 18: CES5-CES1.1-CES1.2 and CES2-CES3-CES6. Bovine CES1, CES2, CES3, CES5 and CES6 shared 39-45% identity with each other, but showed 71-76% identity with each of the five corresponding human CES family members. Phylogeny studies indicated that bovine CES genes originated from five ancestral gene duplication events which predated the eutherian mammalian common ancestor. In addition, a subsequent CES1 gene duplication event is proposed during mammalian evolution prior to the appearance of the Bovidae common ancestor ~ 20 MY ago.

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Expression and Partial Purification of a Recombinant Secretory Form of Human Liver Carboxylesterase

Cited by 12 publications

References 38 publications

Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Mammalian carboxylesterase 5: Comparative biochemistry and genomics

Heterologous expression and characterization of a malathion-hydrolyzing carboxylesterase from a thermophilic bacterium, Alicyclobacillus tengchongensis

Bovine carboxylesterases: Evidence for two CES1 and five families of CES genes on chromosome 18

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