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Literature summary for 4.4.1.1 extracted from

  • Yan, W.; Stone, E.; Zhang, Y.J.
    Structural snapshots of an engineered cystathionine-gamma-lyase reveal the critical role of electrostatic interactions in the active site (2017), Biochemistry, 56, 876-885 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
use of Escherichia coli codon-optimized gene Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of mutant E59N/R119L/E339V with distinct reaction intermediates, including internal aldimine, substrate-bound, gem-diamine, and external aldimine forms. A locally unfolded active site correlates with inhibition of activity as a function of ionic strength Homo sapiens

Protein Variants

Protein Variants Comment Organism
E59N/R119L/E339V mutant engineered as an L-Met-degrading enzyme based on the human cystathionine-gamma-lyase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P32929
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Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate a salt bridge between the phosphate of cofactor pyridoxal 5'-phosphate and residue R62 plays an important role in catalyzing beta- and gamma-eliminations Homo sapiens