[17] Acylaminoacyl-peptidase

Jones, Wanda M.; Scaloni, Andrea; Manning, James M.

doi:10.1016/0076-6879(94)44019-0

Cited by 24 publications

(25 citation statements)

References 10 publications

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“…As previously described, APEH is a ubiquitous cytosolic protein that seems to have an almost universal distribution in all living organisms [21,22,25,26,28,29], although much is still unknown about its biological function. Interestingly, although a unique gene has been found so far for mammalian members of APEH family, searches in different protein databases have revealed the existence of two homologous sequences of APEH in several fish species.…”

Section: Resultsmentioning

confidence: 99%

“…To date, APEH has been studied in a number of eukaryal [22][23][24][25] and archaeal [26][27][28] organisms, and recently in a psychrophilic bacterium, Sporosarcina psychrophila [29,30], but its biological role has not yet been completely elucidated. The crystal structure of POPs shows a peptidase domain with a a/b-hydrolase fold, and an unusual b-propeller, which covers the catalytic triad [20,31].…”

Section: Introductionmentioning

confidence: 99%

“…APEH (also referred as acylaminoacyl peptidase or acylamino-acid-releasing enzyme) is a ubiquitous cytosolic enzyme belonging to the prolyl oligopeptidase (POP) family of serine peptidases (clan SC, family S9) that catalyzes the removal of N a -acetylated amino acids from blocked peptides, acting as a key regulator of N-terminally acetylated proteins in human cells [20][21][22]. To date, APEH has been studied in a number of eukaryal [22][23][24][25] and archaeal [26][27][28] organisms, and recently in a psychrophilic bacterium, Sporosarcina psychrophila [29,30], but its biological role has not yet been completely elucidated.…”

Section: Introductionmentioning

confidence: 99%

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A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii

et al. 2013

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Oxidative challenge is an important factor affecting the adaptive strategies of Antarctic fish, but data on antioxidant defenses in these organisms remain scarce. In this context, a key role could be played by acylpeptide hydrolase (APEH), which was recently hypothesized to participate in the degradation of oxidized and cytotoxic proteins, although its physiological function is still not fully clarified. This study represents the first report on piscine members of this enzyme family, specifically from the Antarctic teleost Trematomus bernacchii. The cDNAs corresponding to two apeh genes were isolated, and the respective proteins were functionally and structurally characterized with the aim of understanding the biological significance of these proteases in Antarctic fish. Both APEH isoforms (APEH-1 Tb and APEH-2 Tb ) showed distinct temperature-kinetic behavior, with significant differences in the K m values. Moreover, beside the typical acylpeptide hydrolase activity, APEH-2 Tb showed remarkable oxidized protein endohydrolase activity towards oxidized BSA, suggesting that this isoform could play a homeostatic role in removing oxidatively damaged proteins, sustaining the antioxidant defense systems. The 3D structures of both APEHs were predicted, and a possible relationship was found between the substrate specificity/affinity and the marked changes in the number of charged residues and hydrophobicity properties surrounding their catalytic sites. Our results demonstrated the occurrence of two APEH isoforms in T. bernacchii, belonging to different phylogenetic clusters, identified for the first time, and showing distinct molecular and temperature-kinetic behaviors. In addition, we suggest that the members of the new cluster 'APEH-2' could participate in reactive oxygen species detoxification as phase 3 antioxidant enzymes, enhancing the protein degradation machinery.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii

et al. 2013

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“…Peptidases find difficulty in cleaving at these modified amino acids. Acylaminoacyl peptidases are enzymes known for hydrolysis of such Nterminally modified amino acids (Jones et al, 1994). Acylaminoacyl peptidases have been purified from different eukaryotic sources like bovine liver, rabit muscle and ovine liver (Farries et al, 1991;Gade and Brown, 1978) and found that these are composed of four identical subunits (Polgár, 2002).…”

Section: Acylaminoacyl Peptidasesmentioning

confidence: 99%

Proteolytic inventory of Thermococcus kodakaraensis

Rasool¹,

Rashid²,

Bashir³

et al. 2013

Afr. J. Microbiol. Res.

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Proteolysis is a very crucial process for development and survival of the cell. Genome sequence data can be employed to estimate proteolysis inventories of different organisms. In this review, we exploit genome sequence data of hyperthermophilic archaeon Thermococcus kodakaraensis to have an overview of the proteolysis in this microorganism. The overview is based on those peptidases that have been characterized, and on putative peptidases that have been identified but have yet to be characterized. In contrast to bacteria, the number of proteolytic enzymes in archaea is quite low. By analyzing the genome sequence data, we tried to establish how T. kodakaraensis maintains its life cycle and other processes by using such a small number of protein scavengers while harboring at high temperature where chances of protein denaturation are high.

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“…Prolyl oligopeptidases bear little sequence resemblance to classic serine proteases such as trypsin and subtilisin except for a consensus motif Gly-X-Ser-X-Gly that contains the active-site serine (Brenner, 1988). As for all serine oligopeptidases, acylaminoacyl peptidase has an active site consisting of three catalytically competent residues, serine, histidine and aspartic acid (Polgá r, 1992;Rawlings et al, 1991;Jones et al, 1994), in this case Ser587, Asp675 and His707. Oligopeptidases select oligopeptide substrates that are comprised of not more than about 30 amino-acid residues.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase

et al. 2005

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Acylaminoacyl peptidase (also known as acylamino-acid-releasing enzyme or acylpeptide hydrolase; EC 3.4.19.1) is an unusual member of the prolyl oligopeptidase family catalysing the hydrolysis of an N-acylated peptide to an acylamino acid and a peptide with a free N-terminus. Acylaminoacyl peptidase purified from porcine liver has been crystallized in mother liquor containing 0.1 M Tris-HCl pH 7.0, 10%(w/v) polyethylene glycol 8000, 50 mM MgCl 2 and 1%(w/v) CHAPS using the hanging-drop vapour-diffusion technique. A full data set to 3.4 Å resolution was collected at ESRF beamline ID14-4 and space group C222 was assigned, with unit-cell parameters a = 84.8, b = 421.1, c = 212.0 Å and four molecules in the asymmetric unit.

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[17] Acylaminoacyl-peptidase

Cited by 24 publications

References 10 publications

A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii

A novel class of bifunctional acylpeptide hydrolases – potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii

Proteolytic inventory of Thermococcus kodakaraensis

Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase

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