Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.1 extracted from

  • Zimmerman, S.; Domsic, J.F.; Tu, C.; Robbins, A.H.; McKenna, R.; Silverman, D.N.; Ferry, J.G.
    Role of Trp19 and Tyr200 in catalysis by the gamma-class carbonic anhydrase from Methanosarcina thermophila (2013), Arch. Biochem. Biophys., 529, 11-17.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion technique Methanosarcina thermophila

Protein Variants

Protein Variants Comment Organism
additional information although Trp19 and Y200 are non-essential, they contribute to an extended active-site structure distant from the catalytic metal that fine tunes catalysis. Trp19 is important for both CO2/bicarbonate interconversion, and the proton transfer step of catalysis Methanosarcina thermophila
W19A kcat/km at pH 7.5 is 2.5fold lower than wild-type value, kcat/km at pH 8.8 is 2.2fold lower than wild-type value Methanosarcina thermophila
W19F kcat/km at pH 7.5 is 5fold lower than wild-type value, kcat/km at pH 8.8 is 5.2fold lower than wild-type value Methanosarcina thermophila
W19N kcat/km at pH 7.5 is 3.2fold lower than wild-type value, kcat/km at pH 8.8 is 2.4fold lower than wild-type value Methanosarcina thermophila
Y200A kcat/km at pH 7.5 is 3.5fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value Methanosarcina thermophila
Y200F kcat/km at pH 7.5 is 3.6fold higher than wild-type value, kcat/km at pH 8.8 is 2.5fold lower than wild-type value Methanosarcina thermophila
Y200S kcat/km at pH 7.5 is 3fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value Methanosarcina thermophila

Organism

Organism UniProt Comment Textmining
Methanosarcina thermophila P40881
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO2 + H2O
-
 Methanosarcina thermophila H2CO3
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5800
-
 CO2 25°C, pH 7.5, mutant enzyme W19N Methanosarcina thermophila
6500
-
 CO2 25°C, pH 7.5, mutant enzyme W19F Methanosarcina thermophila
7900
-
 CO2 25°C, pH 7.5, mutant enzyme W19A Methanosarcina thermophila
32400
-
 CO2 25°C, pH 7.5, wild-type enzyme Methanosarcina thermophila
79300
-
 CO2 25°C, pH 7.5, mutant enzyme Y200S Methanosarcina thermophila
95000
-
 CO2 25°C, pH 7.5, mutant enzyme Y200A Methanosarcina thermophila
120100
-
 CO2 25°C, pH 7.5, mutant enzyme Y200F Methanosarcina thermophila

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
400
-
 CO2 25°C, pH 7.5, mutant enzyme W19F Methanosarcina thermophila
600
-
 CO2 25°C, pH 8.8, mutant enzyme W19F Methanosarcina thermophila
630
-
 CO2 25°C, pH 7.5, mutant enzyme W19N Methanosarcina thermophila
790
-
 CO2 25°C, pH 7.5, mutant enzyme W19A Methanosarcina thermophila
1300
-
 CO2 25°C, pH 8.8, mutant enzyme W19N Methanosarcina thermophila
1400
-
 CO2 25°C, pH 8.8, mutant enzyme W19A Methanosarcina thermophila
2000
-
 CO2 25°C, pH 7.5, wild-type enzyme Methanosarcina thermophila
3100
-
 CO2 25°C, pH 8.8, wild-type enzyme Methanosarcina thermophila
5900
-
 CO2 25°C, pH 7.5, mutant enzyme Y200S Methanosarcina thermophila
7000
-
 CO2 25°C, pH 7.5, mutant enzyme Y200A Methanosarcina thermophila
7100
-
 CO2 25°C, pH 7.5, mutant enzyme Y200F Methanosarcina thermophila
7900
-
 CO2 25°C, pH 8.8, mutant enzyme Y200F Methanosarcina thermophila
10200
-
 CO2 25°C, pH 8.8, mutant enzyme Y200S Methanosarcina thermophila
10300
-
 CO2 25°C, pH 8.8, mutant enzyme Y200A Methanosarcina thermophila