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Literature summary for 4.2.1.109 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

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

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/ Products (Substrates)

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
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q96GX9
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-

Reaction

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 and Products (Substrate)

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
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?

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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assay at Homo sapiens

General Information

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