Protein Variants | Comment | Organism |
---|---|---|
D72A | site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme | Homo sapiens |
D72A/K90A | 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 | Homo sapiens |
K90A | 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 | Homo sapiens |
P185A | site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme | Homo sapiens |
Y184A | site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme | Homo sapiens |
Y184A/P185A | site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | 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 | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-methyl-5-thio-D-ribulose 1-phosphate | Homo sapiens | substrate-binding mode, overview | 5-(methylthio)-2,3-dioxopentyl phosphate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q96GX9 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
5-(methylsulfanyl)-D-ribulose 1-phosphate = 5-(methylsulfanyl)-2,3-dioxopentyl phosphate + H2O | active site architecture and catalytic mechanism, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-methyl-5-thio-D-ribulose 1-phosphate | substrate-binding mode, overview | Homo sapiens | 5-(methylthio)-2,3-dioxopentyl phosphate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
5-methylthioribulose-1-phosphate dehydratase | - |
Homo sapiens |
Apaf-1 interacting protein | - |
Homo sapiens |
APIP | - |
Homo sapiens |
MtnB | - |
Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in the methionine salvage pathway | Homo sapiens |
additional information | active site architecture and catalytic mechanism, overview | Homo sapiens |
physiological function | 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 | Homo sapiens |