Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327

Jajčanin-Jozić, Nina; Macheroux, Peter; Abramić, Marija

doi:10.5562/cca2107

Cited by 2 publications

(2 citation statements)

References 19 publications

(29 reference statements)

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“…An04g01950 from subfamily M48A is provisionally identified as ste24 peptidase, a zinc metalloprotease catalyzing two proteolytic steps in the maturation of the yeast mating pheromone α-factor 102 . In family M49, An04g00410 is putatively identified as dipeptidyl-peptidase III which participates in intracellular peptide metabolism 103 , whereas An01g02980 doesn’t contain the unique hexapeptide linear motif HEXXXH (X represents any amino acid) and may thus unlikely to carry out proteolysis. The single enzyme sequence in family M76 (An05g00110) encodes the mitochondrial inner membrane protease ATP23 with dual function in the processing and assembly of subunit 6 of mitochondrial ATPase 104 .…”

Section: Subdivision Probable Physiological Functions and Active Sitmentioning

confidence: 99%

“…S2f.) 93 , 105 , and An04g00410 in family M49 contains the exceptional zinc ion ligand motif HEXXXH 103 . Most of these enzymes belong to the gluzincins clan which uses a glutamate as the third metal-binding residue 93 , except those from family M41 which are FtsH-like AAA metallopeptidases and An05g00110 from family M76 that can not be assigned into any clan (Supplementary Table S4 ).…”

Section: Subdivision Probable Physiological Functions and Active Sitmentioning

confidence: 99%

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Bioinformatic mapping of a more precise Aspergillus niger degradome

Dong

Yang

Lee

2021

Sci Rep

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Aspergillus niger has the ability to produce a large variety of proteases, which are of particular importance for protein digestion, intracellular protein turnover, cell signaling, flavour development, extracellular matrix remodeling and microbial defense. However, the A. niger degradome (the full repertoire of peptidases encoded by the A. niger genome) available is not accurate and comprehensive. Herein, we have utilized annotations of A. niger proteases in AspGD, JGI, and version 12.2 MEROPS database to compile an index of at least 232 putative proteases that are distributed into the 71 families/subfamilies and 26 clans of the 6 known catalytic classes, which represents ~ 1.64% of the 14,165 putative A. niger protein content. The composition of the A. niger degradome comprises ~ 7.3% aspartic, ~ 2.2% glutamic, ~ 6.0% threonine, ~ 17.7% cysteine, ~ 31.0% serine, and ~ 35.8% metallopeptidases. One hundred and two proteases have been reassigned into the above six classes, while the active sites and/or metal-binding residues of 110 proteases were recharacterized. The probable physiological functions and active site architectures of these peptidases were also investigated. This work provides a more precise overview of the complete degradome of A. niger, which will no doubt constitute a valuable resource and starting point for further experimental studies on the biochemical characterization and physiological roles of these proteases.

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Section: Subdivision Probable Physiological Functions and Active Sitmentioning

confidence: 99%

Section: Subdivision Probable Physiological Functions and Active Sitmentioning

confidence: 99%

Bioinformatic mapping of a more precise Aspergillus niger degradome

Dong

Yang

Lee

2021

Sci Rep

View full text Add to dashboard Cite

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Importance of the three basic residues in the vicinity of the zinc-binding motifs for the activity of the yeast dipeptidyl peptidase III

Jajčanin-Jozić

Tomić

Abramić³

2013

The Journal of Biochemistry

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Yeast dipeptidyl peptidase III (yDPP III) is a member of the metallopeptidase family M49 involved in intracellular protein catabolism. Elucidation of the yDPP III crystal structure has pinpointed the zinc-coordinating residues (two His from H(460)ELLGH(465) motif and the second Glu from E(516)ECRAE(521) motif), and several amino acid residues potentially important for catalytic activity whose roles have not been investigated. Here, three putative catalytic residues of the yDPP III, His578, Arg582 and Lys638 were substituted and the resultant single mutants characterized. The replacement of His578 with an asparagine significantly (122-fold) lowered the catalytic efficiency, kcat/Km, for Arg-Arg-2-naphthylamide (Arg2-2NA) hydrolysis, and affinity for hydroxamate inhibitor Tyr-Phe-NHOH (decline by 14-fold). The R582Q mutant exhibited an order of magnitude higher activity with all four dipeptide derivatives examined, compared to the wild type. The molecular dynamics simulations revealed the change in the H-bond networking in the R582Q variant active-site region. The mutation of Lys638, to Leu, slightly increased the specificity constant for Arg2-2NA hydrolysis. However, the affinity for Tyr-Phe-NHOH, and activity for the substrates with uncharged P2 side chains (Ala-Ala-, Ala-Arg- and Phe-Arg-2NA) were dramatically reduced, indicating the importance of the evolutionary conserved salt bridge Lys(638)-Glu(516) for the modulation of DPP III substrate specificity.

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Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327

Cited by 2 publications

References 19 publications

Bioinformatic mapping of a more precise Aspergillus niger degradome

Bioinformatic mapping of a more precise Aspergillus niger degradome

Importance of the three basic residues in the vicinity of the zinc-binding motifs for the activity of the yeast dipeptidyl peptidase III

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