Structure-function and industrial relevance of bacterial aminopeptidase P
MN Omar, RNZ Raja Abd Rahman, ND Muhd Noor… - Catalysts, 2021 - mdpi.com
Aminopeptidase P (APPro, EC 3.4. 11.9) cleaves N-terminal amino acids from peptides and
proteins where the penultimate residue is proline. This metal-ion-dependent enzyme shares …
proteins where the penultimate residue is proline. This metal-ion-dependent enzyme shares …
Structure of the Prolidase from Pyrococcus furiosus
MJ Maher, M Ghosh, AM Grunden, AL Menon… - Biochemistry, 2004 - ACS Publications
The structure of prolidase from the hyperthermophilic archaeon Pyrococcus furiosus (Pf prol)
has been solved and refined at 2.0 Å resolution. This is the first structure of a prolidase, ie, a …
has been solved and refined at 2.0 Å resolution. This is the first structure of a prolidase, ie, a …
A Molecular Analysis of the Aminopeptidase P-Related Domain of PID-5 from Caenorhabditis elegans
AC Lloyd, KS Gregory, RE Isaac, KR Acharya - Biomolecules, 2023 - mdpi.com
A novel protein, PID-5, has been shown to be a requirement for germline immortality and
has recently been implicated in RNA-induced epigenetic silencing in the Caenorhabditis …
has recently been implicated in RNA-induced epigenetic silencing in the Caenorhabditis …
Aminopeptidase P isozyme expression in human tissues and peripheral blood mononuclear cell fractions
Ç Erşahin, AM Szpaderska, AT Orawski… - Archives of biochemistry …, 2005 - Elsevier
Aminopeptidase P (APP) isoforms specifically remove the N-terminal amino acid from
peptides that have a proline residue in the second position. The mRNA levels of three …
peptides that have a proline residue in the second position. The mRNA levels of three …
Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center
The effect of metal substitution on the activity and structure of the aminopeptidase P (APPro)
from Escherichia coli has been investigated. Measurements of activity in the presence of …
from Escherichia coli has been investigated. Measurements of activity in the presence of …
Catalytic properties of the PepQ prolidase from Escherichia coli
MS Park, CM Hill, Y Li, RK Hardy, H Khanna… - Archives of biochemistry …, 2004 - Elsevier
The PepQ prolidase from Escherichia coli catalyzes the hydrolysis of dipeptide substrates
with a proline residue at the C-terminus. The pepQ gene has been cloned, overexpressed …
with a proline residue at the C-terminus. The pepQ gene has been cloned, overexpressed …
Kinetic and Crystallographic Analysis of Mutant Escherichia coli Aminopeptidase P: Insights into Substrate Recognition and the Mechanism of Catalysis
Aminopeptidase P (APPro) is a manganese-dependent enzyme that cleaves the N-terminal
amino acid from polypeptides where the second residue is proline. APPro shares a similar …
amino acid from polypeptides where the second residue is proline. APPro shares a similar …
[HTML][HTML] Structural basis for the allosteric behaviour and substrate specificity of Lactococcus lactis Prolidase
S Xu, P Grochulski, T Tanaka - … et Biophysica Acta (BBA)-Proteins and …, 2024 - Elsevier
Abstract Prolidase (EC 3.4. 13.9) is an enzyme that specifically hydrolyzes Xaa-Pro
dipeptides into free amino acids. We previously studied kinetic behaviours and solved the …
dipeptides into free amino acids. We previously studied kinetic behaviours and solved the …
Exploring the Antarctic aminopeptidase P from Pseudomonas sp. strain AMS3 through structural analysis and molecular dynamics simulation
Aminopeptidase P (APPro) is a crucial metalloaminopeptidase involved in amino acid
cleavage from peptide N-termini, playing essential roles as versatile biocatalysts with …
cleavage from peptide N-termini, playing essential roles as versatile biocatalysts with …
Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin
SC Graham, MJ Maher, WH Simmons… - … Section D: Biological …, 2004 - journals.iucr.org
Aminopeptidase P (APPro) is a metalloprotease whose active site includes a dinuclear
manganese (II) cluster. The enzyme cleaves the N-terminal residue from a polypeptide when …
manganese (II) cluster. The enzyme cleaves the N-terminal residue from a polypeptide when …