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Literature summary for 2.5.1.6 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
Search for more literature for 2.5.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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]

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

Organic Solvent Stability

Organic Solvent Comment Organism
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

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58605
-
-
Methanocaldococcus jannaschii DSM 2661 Q58605
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanocaldococcus jannaschii

Subunits

Subunits Comment Organism
dimer 2 * 44000 Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
Mj-MAT
-
 Methanocaldococcus jannaschii