This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one . The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]} [1,2].
This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one [2]. The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]} [1,2].
three magnesium ions, one is buried in the active-site pocket in the interface between the two domains, where it serves as a cofactor for the enzyme activity. The other two are located on the surface of the molecule and are supposedly helpful for packing of crystals. Magnesium ions originate from the reservoir solution during crystallization and are absolutely required for the enzyme stability and activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Ischemia
Cerebral Microvascular Endothelial Cell Apoptosis after Ischemia: Role of Enolase-Phosphatase 1 Activation and Aci-Reductone Dioxygenase 1 Translocation.
Cerebral Microvascular Endothelial Cell Apoptosis after Ischemia: Role of Enolase-Phosphatase 1 Activation and Aci-Reductone Dioxygenase 1 Translocation.
exposure of cultured brain microvascular endothelial cells to oxygen-glucose deprivation induced Enoph1 upregulation, which is accompanied by increased cell death and apoptosis. Knockdown of Enoph1 expression or overexpressing Enoph1 attenuates or potentiates oxygen-glucose deprivation-induced endothelial cell death, respectively. Enoph1 knockdown or overexpression results in a significant reduction or augmentation of reactive oxygen species generation, apoptosis-associated proteins and endoplasmic reticulum stress proteins in oxygen-glucose deprivation-treated endothelial cells. Oxygen-glucose deprivation upregulates the expression of Enoph1's downstream protein acireductone dioxygenase 1 and enhances its interaction with Enoph1
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by hanging drop vapour-diffusion method, to 1.7 A resolution, crystals belong to space group P212121, with unit-cell parameters a = 54.02 A, b = 57.55 A, c = 87.32 A
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
focal cerebral ischemia induces Enoph1 mRNA and protein expression in ischemic hemispheric microvessels. Exposure of cultured brain microvascular endothelial cells to oxygen-glucose deprivation also induces Enoph1 upregulation
compared with normal brain tissues, the level of Enoph1 is markedly increased in glioma tissues. The glioma pathological grade is positively associated with the expression level of Enoph1. Knockdown of Enoph1 expression with siRNA markedly reduces cell proliferation, and significantly decreases cell migration. Knockdown of Enoph1 promotes its downstream protein, acireductone dioxygenase 1, to shift from the nucleus to the cytoplasm of U251 glioma cells, while membrane type 1-matrix metalloproteinase expression is significantly downregulated compared with the control group
Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae
Zhang, Y.; Zhang, G.; Zhang, J.; Wang, X.; Wang, J.
Mutagenesis of the enolase-phosphatase gene in Xanthomonas oryzae pv. oryzae affects growth on methylthioadenosine and in vivo S-adenosylmethionine pools
Cerebral microvascular endothelial cell apoptosis after ischemia Role of enolase-phosphatase 1 activation and aci-reductone dioxygenase 1 translocation
3.1.3.77 acireductone synthase
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