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Literature summary extracted from

  • Garrido, F.; Taylor, J.C.; Alfonso, C.; Markham, G.D.; Pajares, M.A.
    Structural basis for the stability of a thermophilic methionine adenosyltransferase against guanidinium chloride (2010), Amino Acids, 42, 361-373.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.6 expression in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.6 W387F the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride Methanocaldococcus jannaschii
2.5.1.6 W387F/Y120W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y170W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y226W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y233W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y255W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y267W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y273W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y323W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a delayed first transition Methanocaldococcus jannaschii
2.5.1.6 W387F/Y344W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition Methanocaldococcus jannaschii
2.5.1.6 W387F/Y371W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a delayed first transition Methanocaldococcus jannaschii
2.5.1.6 W387F/Y49W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme shows a single inactivation transition Methanocaldococcus jannaschii
2.5.1.6 W387F/Y72W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme and mutant enzyme W387F/Y72W in guanidinium chloride is a three-state process. Lower resistance to guanidinium chloride than the wild type enzyme Methanocaldococcus jannaschii
2.5.1.6 W387F/Y85W the mutant is active and dimeric, and shows no dramatic alterations in its affinity for the substrates or far-UV CD spectra due to mutations. Unfolding of the wild-type enzyme in guanidinium chloride is a three-state process in which a dimeric intermediate can be identified. The mutant enzyme exhibits two inactivation transitions in guanidinium chloride Methanocaldococcus jannaschii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.6 44000
-
 2 * 44000 Methanocaldococcus jannaschii

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
2.5.1.6 guanidine-HCl the enzyme is fully and irreversibly unfolded in the presence of guanidinium chloride. Unfolding of this dimeric protein is a three-state process in which a dimeric intermediate can be identified. The less stable secondary structural elements of the protein are the C-terminal ends of beta-strands E2 and E6 Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.6 Methanocaldococcus jannaschii Q58605
-
-
2.5.1.6 Methanocaldococcus jannaschii DSM 2661 Q58605
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.6
-
 Methanocaldococcus jannaschii

Subunits

EC Number Subunits Comment Organism
2.5.1.6 dimer 2 * 44000 Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
2.5.1.6 Mj-MAT
-
 Methanocaldococcus jannaschii