22.214.171.124 - O-phosphoserine sulfhydrylase
H(+) + hydrogen sulfide + O-phospho-L-serine = L-cysteine + phosphate
There are no Reaction Mechanism for this Enzyme
There are no kinetic parameters information for this Enzyme
- Role of F225 in O-phosphoserine sulfhydrylase from Aeropyrum pernix K1.
- O-PHOSPHOSERINE SULFHYDRYLASE VARIANTS
- O-PHOSPHOSERINE SULFHYDRYLASE MUTANTS AND METHOD FOR PRODUCTION OF CYSTEINE USING THE SAME
- O-phosphoserine sulfhydrylase mutants and method for production of cysteine using the same
- Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1.
- Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria.
- Cysteine Biosynthesis in Campylobacter jejuni: Substrate Specificity of CysM and the Dualism of Sulfide.
- The coral Acropora loripes genome reveals an alternative pathway for cysteine biosynthesis in animals.
- Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution.
- Sulfur metabolism in subtropical marine mangrove sediments fundamentally differs from other habitats as revealed by SMDB.
- Combatting antimicrobial resistance via the cysteine biosynthesis pathway in bacterial pathogens.