near the zinc ion, the surface of the active site pocket is formed by several residues, including Cys97, Tyr198, Glu139, Lys142, and Asn166. Residues Cys97, Glu139, and Tyr198 form hydrogen bonds with the three water molecules that coordinate the zinc ion
MtnB requires metal ions for catalysis, but it is unclear what kind of metal ions are bound to the MtnB purified from Escherichia coli cells. Considering that FucA/RibE/RhuA-related enzymes require the zinc ion for optimal catalysis under physiological conditions and that recombinant class II aldolase enzymes expressed in Escherichia coli cells are almost all of the Zn2+ form, purified MtnB might also be of the Zn2+ form
MtnB requires metal ions for catalysis, but it is unclear what kind of metal ions are bound to the MtnB purified from Escherichia coli cells. Considering that FucA/RibE/RhuA-related enzymes require the zinc ion for optimal catalysis under physiological conditions and that recombinant class II aldolase enzymes expressed in Escherichia coli cells are almost all of the Zn2+ form, purified MtnB might also be of the Zn2+ form
Positive regulation of apoptosis by HCA66, a new Apaf-1 interacting protein, and its putative role in the physiopathology of NF1 microdeletion syndrome patients.
the MtnB domain of Tetrahymena thermophila MtnBD acquired the new function to catalyze both the dehydratase and enolase reactions through evolutionary gene mutations, rather than fusion of MSP genes
the enzyme depletion specifically impairs the capacity of cells to grow in media where methionine is replaced by 5-methylthioadenosine. Knockdown of the enzyme specifically affects the recycling of methionine, and mutation of three potential phosphorylation sites does not affect the enzyme activity whereas mutation of the potential zinc binding site completely abrogates it
the MtnBD fusion enzyme in Tetrahymena thermophila catalyzes two of the sequential reactions from the dehydratase to dioxygenase steps in the methionine salvage pathway: 5-methylthioribulose-1-phosphate is converted to 2-oxo-4-methylthiobutyrate, the methionine precursor, by four steps, namely dehydratase, enolase, phosphatase, and dioxygenase reactions. The MtnB domain catalyzes dehydration and enolization and the MtnD domain catalyzes dioxygenation, the phosphatase is distinct from the enzyme. Methionine salvage pathway, overview
Apaf-1-interacting protein (APIP) is known to inhibit two different types of cell death: caspase-1-dependent pyroptosis and caspase-9-dependent apoptosis. The enzyme is also involved in the methionine-salvage pathway, where it is called 5-methylthioribulose-1-phosphate dehydratase (MtnB). The enzyme activity seems to be essential for inhibition of pyroptosis by the enzyme, but not for inhibition of apoptosis, overview
the enzyme Apaf-1 interacting protein/5-methylthioribulose-1-phosphate dehydratase has two distinct functions, cell death inhibition and methionine salvage. It functions as a cell death inhibitor independently of its MtnB enzyme activity for apoptosis, but dependently for caspase-1-induced pyroptosis. Pyroptosis inhibition by the Apaf-1 interacting protein is dependent upon its MtnB enzyme activity. Role of Apaf-1 interacting protein/5-methylthioribulose-1-phosphate dehydratase in development of cancers and inflammatory diseases. The enzyme acts as an inhibitor of caspase-9-dependent apoptosis induced by ischemic/hypoxic injury or by cytotoxic agents such as etoposide and cisplatin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme fragment of residues 20-242, hanging drop vapour diffusion method, 0.001 ml of protein solution, containing 20 mM Tris-HCl, 5% v/v glycerol, 0.1 mM TCEP, 100 mM sodium chloride, pH 8.0, is mixed with 0.001 ml of reservoir solution, containing 0.04 M citric acid, 0.06 M Bis-Tris propane, 5% v/v glycerol, 18-21% w/v PEG 3350, and equilibrated against 0.2 ml of reservoir solution, 22°C, 5 days to 2 weeks, X-ray diffraction structure determination and analysis at 2.40 A resolution
site-directed mutagenesis, the mutant shows a similar level of pyroptosis inhibition as the wild-type enzyme, but a significant loss of apoptosis inhibition activity
site-directed mutagenesis, the mutant shows a similar level of pyroptosis inhibition as the wild-type enzyme, but a significant loss of apoptosis inhibition activity
transient silencing of the enzyme in HeLa cells. Stable knockdown of the enzyme specifically affects growth in 5-methylthioadenosine and depletes intracellular levels of methionine
transient silencing of the enzyme in HeLa cells. Stable knockdown of the enzyme specifically affects growth in 5-methylthioadenosine and depletes intracellular levels of methionine
recombinant His-tagged enzyme residues 20-242 from Escherichia coli strain Rosetta 2(DE3) by metal affinity chhromatography, anion exchange chromatography, gel filtration, and ultrafiltration
gene mtnBD, identification of the domains responsible for catalyzing the four reactions from the enzyme, overview. Recombinant expression of His-tagged proteins of full-length enzyme and the MtnB domain in Escherichia coli BL21(DE3)