Anaerobic sulfatase maturase AslB from Escherichia coli activates human recombinant iduronate-2-sulfate sulfatase (IDS) and N-acetylgalactosamine-6-sulfate sulfatase (GALNS)

Maturation of type I sulfatases requires the conversion of the cysteine (Cys) or serine (Ser) present in the active site to formylglycine (FGly). This activation represents a limiting step during the production of recombinant sulfatases in bacteria and eukaryotic hosts. AslB, YdeM and YidF have been...

Full description

Autores:
Tipo de recurso:
Fecha de publicación:
2017
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/24133
Acceso en línea:
https://doi.org/10.1016/j.gene.2017.08.043
https://repository.urosario.edu.co/handle/10336/24133
Palabra clave:
Anaerobic sulfatase maturase aslb
Cysteine
Iduronate 2 sulfatase
N acetylgalactosamine 6 sulfatase
Recombinant enzyme
Serine
Sulfatase
Unclassified drug
Escherichia coli protein
Glycoprotein
N acetylgalactosamine 4 sulfatase
Protein binding
Recombinant protein
Sulfatase
Amino acid sequence
Article
Binding affinity
Controlled study
Enzyme activation
Enzyme active site
Enzyme activity
Escherichia coli
Molecular docking
Molecular dynamics
Molecular model
Nonhuman
Priority journal
Protein expression
Protein motif
Protein protein interaction
Chemistry
Enzyme activation
Enzymology
Escherichia coli
Human
Metabolism
Catalytic Domain
Chondroitinsulfatases
Cysteine
Enzyme Activation
Escherichia coli
Escherichia coli Proteins
Glycoproteins
Humans
Molecular Docking Simulation
Molecular Dynamics Simulation
Protein Binding
Recombinant Proteins
Serine
Sulfatases
Aslb
Formylglycine-generating enzymes
Iduronate-2-sulfate sulfatase
N-acetylgalactosamine-6-sulfate sulfatase
Sulfatases
human
human
Molecular
GALNS protein
IDS protein
Models
Rights
License
Abierto (Texto Completo)