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

BRENDA support

Literature summary 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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.1 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
4.2.1.1 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
4.2.1.1 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
4.2.1.1 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
4.2.1.1 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
4.2.1.1 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
4.2.1.1 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

EC Number Organism UniProt Comment Textmining
4.2.1.1 Methanosarcina thermophila P40881
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.1 5800
-
CO2 25°C, pH 7.5, mutant enzyme W19N Methanosarcina thermophila
4.2.1.1 6500
-
CO2 25°C, pH 7.5, mutant enzyme W19F Methanosarcina thermophila
4.2.1.1 7900
-
CO2 25°C, pH 7.5, mutant enzyme W19A Methanosarcina thermophila
4.2.1.1 32400
-
CO2 25°C, pH 7.5, wild-type enzyme Methanosarcina thermophila
4.2.1.1 79300
-
CO2 25°C, pH 7.5, mutant enzyme Y200S Methanosarcina thermophila
4.2.1.1 95000
-
CO2 25°C, pH 7.5, mutant enzyme Y200A Methanosarcina thermophila
4.2.1.1 120100
-
CO2 25°C, pH 7.5, mutant enzyme Y200F Methanosarcina thermophila

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.2.1.1 400
-
CO2 25°C, pH 7.5, mutant enzyme W19F Methanosarcina thermophila
4.2.1.1 600
-
CO2 25°C, pH 8.8, mutant enzyme W19F Methanosarcina thermophila
4.2.1.1 630
-
CO2 25°C, pH 7.5, mutant enzyme W19N Methanosarcina thermophila
4.2.1.1 790
-
CO2 25°C, pH 7.5, mutant enzyme W19A Methanosarcina thermophila
4.2.1.1 1300
-
CO2 25°C, pH 8.8, mutant enzyme W19N Methanosarcina thermophila
4.2.1.1 1400
-
CO2 25°C, pH 8.8, mutant enzyme W19A Methanosarcina thermophila
4.2.1.1 2000
-
CO2 25°C, pH 7.5, wild-type enzyme Methanosarcina thermophila
4.2.1.1 3100
-
CO2 25°C, pH 8.8, wild-type enzyme Methanosarcina thermophila
4.2.1.1 5900
-
CO2 25°C, pH 7.5, mutant enzyme Y200S Methanosarcina thermophila
4.2.1.1 7000
-
CO2 25°C, pH 7.5, mutant enzyme Y200A Methanosarcina thermophila
4.2.1.1 7100
-
CO2 25°C, pH 7.5, mutant enzyme Y200F Methanosarcina thermophila
4.2.1.1 7900
-
CO2 25°C, pH 8.8, mutant enzyme Y200F Methanosarcina thermophila
4.2.1.1 10200
-
CO2 25°C, pH 8.8, mutant enzyme Y200S Methanosarcina thermophila
4.2.1.1 10300
-
CO2 25°C, pH 8.8, mutant enzyme Y200A Methanosarcina thermophila