Backbone dynamics of Escherichia coli thioesterase/protease I: evidence of a flexible active-site environment for a serine protease 1 1Edited by M. F. Summers

Huang, Yu‐Huei; Liaw, Yen-Chywan; Gorbatyuk, Vitaliy; Huang, Tai Huang

doi:10.1006/jmbi.2001.4539

Cited by 48 publications

(23 citation statements)

References 63 publications

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“…TAPI displayed multifunctional activity as protease, thioesterase, arylesterase and lysophospholipase (Lee et al 1997). At molecular level, this catalytic multifunctionality was explained by a structurally Xexible active site allowing diVerent substrates to bind in optimal conformations for catalysis to occur (Huang et al 2001). …”

Section: Evolutionmentioning

confidence: 99%

Sinapate esters in brassicaceous plants: biochemistry, molecular biology, evolution and metabolic engineering

Milkowski

Strack

2010

Planta

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Brassicaceous plants are characterized by a pronounced metabolic flux toward sinapate, produced by the shikimate/phenylpropanoid pathway, which is converted into a broad spectrum of O-ester conjugates. The abundant sinapate esters in Brassica napus and Arabidopsis thaliana reflect a well-known metabolic network, including UDP-glucose:sinapate glucosyltransferase (SGT), sinapoylglucose:choline sinapoyltransferase (SCT), sinapoylglucose:L-malate sinapoyltransferase (SMT) and sinapoylcholine (sinapine) esterase (SCE). 1-O-Sinapoylglucose, produced by SGT during seed development, is converted to sinapine by SCT and hydrolyzed by SCE in germinating seeds. The released sinapate feeds via sinapoylglucose into the biosynthesis of sinapoylmalate in the seedlings catalyzed by SMT. Sinapoylmalate is involved in protecting the leaves against the deleterious effects of UV-B radiation. Sinapine might function as storage vehicle for ready supply of choline for phosphatidylcholine biosynthesis in young seedlings. The antinutritive character of sinapine and related sinapate esters hamper the use of the valuable seed protein of the oilseed crop B. napus for animal feed and human nutrition. Due to limited variation in seed sinapine content within the assortment of B. napus cultivars, low sinapine lines cannot be generated by conventional breeding giving rise to genetic engineering of sinapate ester metabolism as a promising means. In this article we review the progress made throughout the last decade in identification of genes involved in sinapate ester metabolism and characterization of the encoded enzymes. Based on gene structures and enzyme recruitment, evolution of sinapate ester metabolism is discussed. Strategies of targeted metabolic engineering, designed to generate low-sinapate ester lines of B. napus, are evaluated.

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Section: Evolutionmentioning

confidence: 99%

Sinapate esters in brassicaceous plants: biochemistry, molecular biology, evolution and metabolic engineering

Milkowski

Strack

2010

Planta

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“…Sequence comparisons suggest that these ORFs encode proteins most closely related to a part of the ORF1 proteins of several vertebrate retroposons, such as CR1 from the chicken (Haas et al, 1997) and Maui from the pufferfish Fugu rubripes (Poulter et al, 1999). The sequence is also related to a variety of cellular enzymes, including TEP-I (Thioesterase I/ Protease I) from E. coli (Huang et al, 2001). The function of this ORF has not yet been determined.…”

Section: Ngaro-like Elements From Amphibia: Xlngaromentioning

confidence: 99%

DIRS-1 and the other tyrosine recombinase retrotransposons

Poulter

Goodwin

2005

Cytogenet Genome Res

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DIRS-1 is a retroelement from the slime mold Dictyostelium discoideum. Until recently only two related retrotransposons had been described: PAT from the nematode Panagrellus redivivus and Prt1 from the zygomycete fungus Phycomyces blakesleeanus. Analyses of the reverse transcriptase sequences encoded by these three elements suggested that they were closely related to each other and more distantly related to the Ty3/gypsy Long Terminal Repeat (LTR) retroelements. They have several unusual structural features that distinguish them from typical LTR elements. For instance, they each encode a tyrosine recombinase (YR), but not a DDE-type integrase or an aspartic protease. Although the DIRS-1-related elements are bordered by terminal repeats these differ from typical LTRs in a number of ways. In DIRS-1, for example, the terminal repeats are inverted (complementary), non-identical in sequence, and the outer edges of the terminal sequences are repeated (adjacent to each other) in the internal region. PAT has so-called “split” direct repeats in which the unrelated terminal sequences appear as direct repeats adjacent to each other in the internal region. The only repetition displayed by Prt1 is the presence of short inverted terminal repeats, but the sequenced copy of this element is believed to be a truncated version of an element with a structure resembling DIRS-1. The unusual structure of the terminal repeats of the DIRS1-like elements appears to be related to their replication via free circular intermediates. Site-specific recombination is believed to integrate the circle without creating duplications of the target sites. In recognition of these important distinctions it is proposed that the retrotransposons that encode tyrosine recombinases be called the tyrosine recombinase (or YR) retrotransposons. Recently a large number of additional YR retrotransposons have been described, including elements from fungi (zygomycetes and basidiomycetes), plants (green algae) and a wide range of animals including nematodes, insects, sea urchins, fish and amphibia, while remnants of elements related to DIRS-1 occur in the human genome. The complete set of YR retrotransposons can be divided into two major groups, the DIRS elements and the Ngaro elements, the two groups forming distinct clades on phylogenetic trees based on alignments of RT/RH and recombinase sequences, and also having some structural distinctions. A third group of transposable elements, which we call Cryptons, also carry tyrosine recombinases. These elements do not encode a reverse transcriptase and so are believed to be DNA transposons not retrotransposons. They have been detected in several pathogenic fungi, including the basidiomycete Cryptococcus neoformans, and the ascomycetes Coccidioides posadasii and Histoplasma capsulatum. Sequence comparisons suggest that the Crypton YRs are related to those of the YR retrotransposons. We suggest that the YR retrotransposons arose from the combination of a Crypton-like YR DNA transposon and the RT/RH encoding sequence of a ...

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“…Es- ter hydrolysis by an endopeptidase is not an unusual feature, since the catalytic triad in ␣/␤ hydrolases, comprising a nucleophile, an acidic residue, and a conserved histidine, enables different types of reactions, including carboxyl ester hydrolysis and peptide hydrolysis (16,45). No carboxypeptidase activity was detectable with three different N-blocked furylacryloyl dipeptides that have been used as substrates for carboxypeptidases B, U, N, or Y.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a Novel Intracellular Endopeptidase of the α/β Hydrolase Family from Streptomyces coelicolor A3(2)

Nagy

Banerjee²,

Tamura

et al. 2003

J Bacteriol

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In a proteasome-lacking mutant of Streptomyces coelicolor A3(2), an intracellular enzyme with chymotrypsinlike activity, absent from the wild type, was detected. Complementation that restored proteasome function did not suppress expression of the endopeptidase. Since the enzyme was not found in two other S. coelicolor proteasome mutants, its expression probably resulted from a secondary mutation arisen in the proteasome mutant. Purification of the endopeptidase revealed its identity to SCO7095, a putative hydrolase encoded by the S. coelicolor A3(2) genome with no known homologue. Based on the prediction of a Ser-Asp-His catalytic triad and an ␣/␤ hydrolase fold, SCO7095 was assigned to peptidase clan SC. N-terminally His-tagged SCO7095 was efficiently expressed in Escherichia coli cells and purified for further characterization. Although SCO7095 is distantly related to several proline iminopeptidases, including Thermoplasma acidophilum tricorn-interacting F1, no aminopeptidase activity was detected. On synthetic substrates, the monomeric enzyme exhibited not only chymotrypsin-like activity but also thrombin-like activity.

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Backbone dynamics of Escherichia coli thioesterase/protease I: evidence of a flexible active-site environment for a serine protease 1 1Edited by M. F. Summers

Cited by 48 publications

References 63 publications

Sinapate esters in brassicaceous plants: biochemistry, molecular biology, evolution and metabolic engineering

Sinapate esters in brassicaceous plants: biochemistry, molecular biology, evolution and metabolic engineering

DIRS-1 and the other tyrosine recombinase retrotransposons

Characterization of a Novel Intracellular Endopeptidase of the α/β Hydrolase Family from Streptomyces coelicolor A3(2)

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