Literature summary for 3.4.23.21 extracted from

Flentke, G.R.; Glinski, J.; Satyshur, K.; Rich, D.H.
Purification and crystallization of rhizopuspepsin: the use of nickel chelation chromatography to select for catalytically active species (1999), Protein Expr. Purif., 16, 213-220.

Search for more literature for 3.4.23.21

Cloned(Commentary)

Cloned (Comment)	Organism
rhizopuspepsinogen gene transformed into Escherichia coli DH5-alpha	Rhizopus sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals with typical dimensions of 0.3 x 0.3 x 0.6 mm, orthorhombic crystals, space group P2(1)2(1)2(1), with dimensions a : 60.18A, b : 71.10A, and c : 81.21A	Rhizopus sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0034	-	KPVSY(NO2)FRL	pH 7.4, 37°C	Rhizopus sp.

Organism

Organism	UniProt	Comment	Textmining
Rhizopus sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
proenzyme	Rhizopus sp.

Storage Stability

Storage Stability	Organism
-20°C, pure rhizopuspepsin can be stored frozen for at least 4 months	Rhizopus sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
KPVSY(NO2)FRL + H2O	-	Rhizopus sp.	?	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
55	-	KPVSY(NO2)FRL	pH 7.4, 37°C	Rhizopus sp.

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Release 2023.1 (January 2023)