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Literature summary extracted from

  • Kang, W.; Hong, S.H.; Lee, H.M.; Kim, N.Y.; Lim, Y.C.; Le, L.T.M.; Lim, B.; Kim, H.C.; Kim, T.Y.; Ashida, H.; Yokota, A.; Hah, S.S.; Chun, K.H.; Jung, Y.K.; Yang, J.K.
    Structural and biochemical basis for the inhibition of cell death by APIP, a methionine salvage enzyme (2014), Proc. Natl. Acad. Sci. USA, 111, E54-E61.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.109 D72A site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme Homo sapiens
4.2.1.109 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
4.2.1.109 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
4.2.1.109 P185A site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme Homo sapiens
4.2.1.109 Y184A site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme Homo sapiens
4.2.1.109 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

EC Number Metals/Ions Comment Organism Structure
4.2.1.109 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate Homo sapiens substrate-binding mode, overview 5-(methylthio)-2,3-dioxopentyl phosphate + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.109 Homo sapiens Q96GX9
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.109 5-(methylsulfanyl)-D-ribulose 1-phosphate = 5-(methylsulfanyl)-2,3-dioxopentyl phosphate + H2O active site architecture and catalytic mechanism, overview Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate substrate-binding mode, overview Homo sapiens 5-(methylthio)-2,3-dioxopentyl phosphate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.109 5-methylthioribulose-1-phosphate dehydratase
-
 Homo sapiens
4.2.1.109 Apaf-1 interacting protein
-
 Homo sapiens
4.2.1.109 APIP
-
 Homo sapiens
4.2.1.109 MtnB
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.109 7.5
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
4.2.1.109 metabolism the enzyme is involved in the methionine salvage pathway Homo sapiens
4.2.1.109 additional information active site architecture and catalytic mechanism, overview Homo sapiens
4.2.1.109 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