scholarly journals Closer to biochemical events of enzyme maturation

2015 ◽  
Vol 112 (11) ◽  
pp. vi-vi
Keyword(s):  
Enzyme Maturation

Unique insertions within Plasmodium falciparum subtilisin-like protease-1 are crucial for enzyme maturation and activity

2005 ◽  
Vol 144 (2) ◽  
pp. 187-197 ◽  
Author(s):  
Létitia Jean ◽  
Chrislaine Withers-Martinez ◽  
Fiona Hackett ◽  
Michael J. Blackman
Keyword(s):  
Plasmodium Falciparum ◽  
Enzyme Maturation

scholarly journals The Pharmacogenetics of NAT2 Enzyme Maturation in Perinatally HIV Exposed Infants Receiving Isoniazid

2012 ◽  
Vol 52 (4) ◽  
pp. 511-519 ◽  
Author(s):  
Rui Zhu ◽  
Jennifer J. Kiser ◽  
Heiner I. Seifart ◽  
Cedric J. Werely ◽  
Charles D. Mitchell ◽  
...  
Keyword(s):  
Hiv Exposed Infants ◽  
Enzyme Maturation ◽  
Hiv Exposed

Transport and proteolytic processing of rabbit cardiac cathepsin D

1985 ◽  
Vol 248 (1) ◽  
pp. C135-C144
Author(s):  
A. M. Samarel ◽  
A. G. Ferguson ◽  
S. W. Worobec ◽  
M. Lesch
Keyword(s):  
Gel Electrophoresis ◽  
Cathepsin D ◽  
Polyacrylamide Gel Electrophoresis ◽  
Active Form ◽  
Sodium Dodecyl ◽  
Limited Proteolysis ◽  
Proteolytic Processing ◽  
Time Dependent ◽  
Low Density ◽  
Enzyme Maturation

Rabbit cardiac cathepsin D is synthesized as a 53,000-mol wt precursor that undergoes limited proteolysis at an unknown intracellular site to a 48,000-mol wt active form. To examine the site of proteolytic processing, isolated perfused rabbit hearts were fractionated by differential centrifugation 150 or 300 min after pulse labeling with [35S]methionine. Newly synthesized precursor and processed cathepsin D were quantitatively isolated from each fraction by extraction, immunoadsorption, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. After 30-min pulse perfusions, all of the 35S-labeled cathepsin D was present as precursor, with the greatest amounts found in low-density subcellular fractions. Proteolytic processing of cathepsin D precursor occurred after chase perfusions that were coincident with the subcellular redistribution of newly synthesized enzyme from sites of synthesis to heavier subcellular structures. Pulse-chase perfusions with chloroquine (10 microM) inhibited precursor proteolytic processing and the time-dependent subcellular redistribution of newly synthesized cathepsin D. The data are consistent with a model for cardiac lysosomal enzyme maturation in which limited proteolytic processing occurs coincident with or soon after the transport of precursors to an acidic intracellular compartment. The results thus suggest that cathepsin D proteolytic processing occurs within cardiac lysosomes.

scholarly journals A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria

2019 ◽  
Vol 111 (6) ◽  
pp. 1592-1603 ◽  
Author(s):  
Benjamin J. Pinchbeck ◽  
Manuel J. Soriano‐Laguna ◽  
Matthew J. Sullivan ◽  
Victor M. Luque‐Almagro ◽  
Gary Rowley ◽  
...  
Keyword(s):  
Redox Enzyme ◽  
Dual Functional ◽  
Enzyme Maturation ◽  
Maturation Protein ◽  
Nitrate Reductases

From Enzyme Maturation to Synthetic Chemistry: The Case of Hydrogenases

2015 ◽  
Vol 48 (8) ◽  
pp. 2380-2387 ◽  
Author(s):  
Vincent Artero ◽  
Gustav Berggren ◽  
Mohamed Atta ◽  
Giorgio Caserta ◽  
Souvik Roy ◽  
...  
Keyword(s):  
Synthetic Chemistry ◽  
Enzyme Maturation

Elucidating the role of the axial cysteine residue in NHase catalysis and the enzyme maturation

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Irene Ogutu ◽  
Wasantha K. P. Lankathilaka ◽  
Richard C. Holz ◽  
Brian A. Bennett
Keyword(s):  
Cysteine Residue ◽  
Enzyme Maturation

scholarly journals Host cell factor requirement for hepatitis C virus enzyme maturation

2001 ◽  
Vol 98 (24) ◽  
pp. 13931-13935 ◽  
Author(s):  
L. Waxman ◽  
M. Whitney ◽  
B. A. Pollok ◽  
L. C. Kuo ◽  
P. L. Darke
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Host Cell ◽  
Host Cell Factor ◽  
Enzyme Maturation

scholarly journals ‘Come into the fold’: A comparative analysis of bacterial redox enzyme maturation protein members of the NarJ subfamily

2014 ◽  
Vol 1838 (12) ◽  
pp. 2971-2984 ◽  
Author(s):  
Catherine S. Chan ◽  
Denice C. Bay ◽  
Thorin G.H. Leach ◽  
Tara M.L. Winstone ◽  
Lalita Kuzniatsova ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Redox Enzyme ◽  
Enzyme Maturation ◽  
Maturation Protein
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