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Literature summary for 1.13.11.91 extracted from

  • Sardar, S.; Weitz, A.; Hendrich, M.P.; Pierce, B.S.
    Outer-sphere tyrosine 159 within the 3-mercaptopropionic acid dioxygenase S-H-Y motif gates substrate-coordination denticity at the non-heme iron active site (2019), Biochemistry, 58, 5135-5150 .
    View publication on PubMed
Search for more literature for 1.13.11.91

Protein Variants

Protein Variants Comment Organism
H157N over 3fold reduction in kcat/Km value Azotobacter vinelandii
Y159F 3fold reduction in kcat/Km value. Fe coordination of cysteine is switched from thiolate only to bidentate (thiolate/amine) for the variant Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.009
-
 3-Mercaptopropanoate mutant Y159F, 37°C, pH not specified in the publication Azotobacter vinelandii
0.012
-
 3-Mercaptopropanoate mutant H157N, 37°C, pH not specified in the publication Azotobacter vinelandii
0.013
-
 3-Mercaptopropanoate wild-type, 20°C, pH not specified in the publication Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-mercaptopropanoate + O2
-
 Azotobacter vinelandii 3-sulfinopropanoate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.081
-
 3-Mercaptopropanoate mutant Y159F, 37°C, pH not specified in the publication Azotobacter vinelandii
0.092
-
 3-Mercaptopropanoate mutant H157N, 37°C, pH not specified in the publication Azotobacter vinelandii
0.45
-
 3-Mercaptopropanoate wild-type, 20°C, pH not specified in the publication Azotobacter vinelandii

General Information

General Information Comment Organism
physiological function a network of hydrogen bonds connects residues H157-Y159 and Fe-bound ligands within the enzymatic Fe site. The hydroxyl group of Y159 hydrogen bonds to Fe-bound NO and, by extension, Fe-bound oxygen during native catalysis. This interaction alters both the NO binding affinity and rhombicity of the 3-mercaptopropanoate-bound iron-nitrosyl site Azotobacter vinelandii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
7.8
-
 3-Mercaptopropanoate mutant H157N, 37°C, pH not specified in the publication Azotobacter vinelandii
9
-
 3-Mercaptopropanoate mutant Y159F, 37°C, pH not specified in the publication Azotobacter vinelandii
27
-
 3-Mercaptopropanoate wild-type, 20°C, pH not specified in the publication Azotobacter vinelandii