Literature summary for 3.4.21.59 extracted from

Marquardt, U.; Zettl, F.; Huber, R.; Bode, W.; Sommerhoff, C.
The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region (2002), J. Mol. Biol., 321, 491-502.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Pichia pastoris yeast system pPICZa	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
2.2 A crystal structure of mature alpha1-tryptase, crytallized by vapor diffusion method, space group P2(1)2(1)2(1), with unit cell dimensions of a = 91.44 A, b = 110.69 A, c = 130.09 A	Homo sapiens

General Stability

General Stability	Organism
mature alpha1-tryptase does not require heparin-binding for stability	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
secretory granule	-	Homo sapiens	30141	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
120000	-	alpha1-tryptase, X-ray exposure	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	human	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant alpha1-tryptase	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	unlike beta-tryptases, alpha-tryptases apparently are proteolytically inactive	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
tetramer	alpha1-tryptase	Homo sapiens

Synonyms

Synonyms	Comment	Organism
alpha 1-tryptase	-	Homo sapiens

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Release 2023.1 (January 2023)