Literature summary for 3.4.17.15 extracted from

Villanueva, J.; Canals, F.; Villegas, V.; Querol, E.; Aviles, F.X.
Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins (2000), FEBS Lett., 472, 27-33.

Search for more literature for 3.4.17.15

Protein Variants

Protein Variants	Comment	Organism
additional information	differential comparison of the activation domain of the proenzyme with three site-directed mutants of different conformational stability by determination of hydrogen exchange using deuterated MALDI-TOF mass spectrometry, overview	Homo sapiens

General Stability

General Stability	Organism
the denaturation with 5 M urea is fully reversible at pH 7.0, the enzyme shows a two state folding transition	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
potato carboxypeptidase inhibitor	determination of hydrogen exchange in the slow exchange core of the inhibitor in different conformational stages using deuterated matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
the denaturation with 5 M urea is fully reversible at pH 7.0, the enzyme shows a two state folding transition	Homo sapiens

Subunits

Subunits	Comment	Organism
More	differential comparison of the activation domain of the proenzyme with three site-directed mutants of different conformational stability by determination of hydrogen exchange using deuterated MALDI-TOF mass spectrometry, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ADA2	-	Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
90	-	3 h, denturation, wild-type and mutant enzymes, determination of hydrogen exchange, after 30 min at room temperature prior to 10fold dilution with proton containing buffer, two mutants fail to denature	Homo sapiens

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Release 2023.1 (January 2023)