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Literature summary extracted from

  • Almog, O.; Kogan, A.; de Leeuw, M.; Gdalevsky, G.Y.; Cohen-Luria, R.; Parola, A.H.
    Structural insights into cold inactivation of tryptophanase and cold adaptation degrees of subtilisin S41: Minireview (2008), Biopolymers, 89, 354-359.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.62
-
 Bacillus amyloliquefaciens
3.4.21.62
-
 Bacillus licheniformis
3.4.21.62 high content of acidic residues mainly found on its surface, making it charged Vibrio sp.
3.4.21.62 subtilisin S41 surface is rich in hydrophilic residues, particularly Asp, which may contribute to its adaptation to psychrophilic conditions Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.62 Ca2+ two binding sites, important for correct folding Bacillus amyloliquefaciens
3.4.21.62 Ca2+ three binding sites, important for correct folding Bacillus licheniformis
3.4.21.62 Ca2+ five binding sites, important for correct folding Bacillus subtilis
3.4.21.62 Ca2+ five binding sites, important for correct folding Lysinibacillus sphaericus
3.4.21.62 Ca2+ three binding sites, important for correct folding Vibrio sp.
4.1.99.1 K+ monovalent cation required for activity and for tight cofactor binding Escherichia coli
4.1.99.1 NH4+ monovalent cation required for activity and for tight cofactor binding Escherichia coli
4.1.99.1 Tl+ monovalent cation required for activity and for tight cofactor binding Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.99.1 52000
-
 4 * 52000 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.1 L-Trp + H2O Escherichia coli
-
 indole + pyruvate + NH4+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.62 Bacillus amyloliquefaciens P00782
-
-
3.4.21.62 Bacillus licheniformis
-
-
-
3.4.21.62 Bacillus subtilis
-
-
-
3.4.21.62 Bacillus subtilis TA41
-
-
-
3.4.21.62 Lysinibacillus sphaericus
-
-
-
3.4.21.62 Vibrio sp. Q8GB52
-
-
4.1.99.1 Escherichia coli P0A853
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.1 L-Trp + H2O
-
 Escherichia coli indole + pyruvate + NH4+
-
 r

Subunits

EC Number Subunits Comment Organism
3.4.21.62 monomer
-
 Bacillus subtilis
3.4.21.62 monomer
-
 Vibrio sp.
4.1.99.1 dimer inactive dimer formed upon cold incubation, process reversible Escherichia coli
4.1.99.1 tetramer 4 * 52000 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.4.21.62 subtilisin BPN’
-
 Bacillus amyloliquefaciens
3.4.21.62 Subtilisin S41
-
 Bacillus subtilis
3.4.21.62 subtilisin Sph
-
 Lysinibacillus sphaericus
3.4.21.62 subtilisin-like protease
-
 Vibrio sp.
3.4.21.62 thermitase
-
 Bacillus licheniformis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.21.62 additional information
-
 cold adapted, negatively charged residues on the surface may be responsible for cold adaptation Bacillus subtilis
3.4.21.62 additional information
-
 mesophilic Bacillus amyloliquefaciens
3.4.21.62 additional information
-
 thermophilic Bacillus licheniformis
3.4.21.62 additional information
-
 cold adapted, negatively charged residues on the surface may be responsible for cold adaptation Vibrio sp.
3.4.21.62 additional information
-
 cold adapted, negatively charged residues on the surface may be responsible for cold adaptation Lysinibacillus sphaericus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.99.1 2
-
 reversible inactivation followed by a dissociation into dimers Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.21.62 additional information does not depend on a cofactor Bacillus subtilis
3.4.21.62 additional information does not depend on a cofactor Vibrio sp.
4.1.99.1 pyridoxal 5'-phosphate
-
 Escherichia coli