Literature summary for 3.4.21.59 extracted from

Rohr, K.B.; Selwood, T.; Marquardt, U.; Huber, R.; Schechter, N.M.; Bode, W.; Than, M.E.
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-beta-tryptase transition (2006), J. Mol. Biol., 357, 195-209.

Search for more literature for 3.4.21.59

Cloned(Commentary)

Cloned (Comment)	Organism
expression of alphaI-tryptase mutants in insect cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
co-crystallization of free and of leupeptin-complexed alphaI-tryptase mutants, 12 mg/ml protein in 10 mM Mops, pH 6.8, 0.7 M NaCl and 0.2 mM leupeptin at room temperature, sitting drop vapor diffusion method, equilibration against reservoir buffer containing 28% PEG 1500, 2 weeks, X-ray diffraction structure determination and anaylsis at 1.6 A resolution, molecular replacement	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D216G	site-directed mutagenesis, alphaI-tryptase mutant, crystal structure determination and analysis, the sole mutation of Asp216 to Gly produces a protease with catalytic and instability properties intermediate between those of alpha and beta-tryptases	Homo sapiens
K192Q	site-directed mutagenesis, alphaI-tryptase mutant, crystal structure determination and analysis, the single mutation of Lys192 to Gln had no effect on activity or enzyme stability	Homo sapiens
K192Q/D216G	site-directed mutagenesis, alphaI-tryptase mutant, crystal structure determination and analysis	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
leupeptin	binding structure with alpha- and beta-tryptase, overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant alphaI-tryptase mutants from insect cells	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
mast cell	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	beta-tryptase is a tetramer that has enzymatic activity, but requires heparin binding to maintain functional and structural stability, alpha-tryptase has little, if any, enzymatic activity but is a stable tetramer in the absence of heparin, both forms are in a two-state equilibrium, which is influenced by the residues in the vicinity of the active site and by inhibitor/substrate binding, substrate binding structure, overview, Asp216 and Lys192 are the main determinants of tryptase activity	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
tetramer	beta-tryptase is a tetramer that has enzymatic activity, but requires heparin binding to maintain functional and structural stability, alpha-tryptase has little, if any, enzymatic activity, probably due to a cryptic active site, but is a stable tetramer in the absence of heparin, both forms are in a two-state equilibrium, which is influenced by the residues in the vicinity of the active site and by inhibitor/substrate binding, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
alpha-tryptase	-	Homo sapiens
beta-tryptase	-	Homo sapiens
tryptase alpha	-	Homo sapiens
tryptase beta	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)