EC Number |
General Information |
Reference |
---|
3.5.1.124 | evolution |
enzyme YajL belongs to the PfpI/Hsp31/DJ-1 superfamily |
739997 |
3.5.1.124 | evolution |
enzyme YhbO belongs to the PfpI/Hsp31/DJ-1 superfamily |
739997 |
3.5.1.124 | evolution |
Hsp31 is a member of the PfpI/Hsp31/DJ-1 superfamily whose members possess a conserved exposed cysteine involved in environmental stress resistance |
739995 |
3.5.1.124 | evolution |
the enzyme PfpI belongs to the PfpI/Hsp31/DJ-1 superfamily |
739999 |
3.5.1.124 | malfunction |
bacterial extracts from a hchA mutant display increased glycation levels and the apparent glyoxylase activity of Hsp31 reflects its deglycase activity |
739995 |
3.5.1.124 | malfunction |
bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. yajL mutants display decreased viability in methylglyoxal- or glucose-containing media |
739997 |
3.5.1.124 | malfunction |
bacterial extracts from deglycase mutants display increased glycation levels, whereas deglycase overexpression decreases protein glycation. yhbO mutants display decreased viability in methylglyoxal- or glucose-containing media |
739997 |
3.5.1.124 | malfunction |
methylglyoxal causes formation of advanced glycation end-products on proteins, one of which is Nepsilon-carboxymethyllysine (CEL), which can be detected by immunoblotting whole cell lysates. Control S2 cells show little to no increase in CEL adducts when treated with 1 mM methylglyoxal. They are capable of efficiently detoxifying methylglyoxal. Knockdown of glyoxalase Glo1 causes a detectable impairment of methylglyoxal detoxification activity in vivo, since CEL adducts are clearly increased upon treatment with 1 mM methylglyoxal. In contrast, DJ-1 knockdown causes no detectable increase in CEL adducts compared with control cells, and combined knockdown of DJ-1beta and Glo1 shows no additional phenotype compared with Glo1 knockdown alone |
740762 |
3.5.1.124 | malfunction |
protein glycation levels are 2 to 10fold increased in deglycase-depleted cells, and deglycase mutants display up to 500fold loss of viability in methylglyoxal or glucose-containing media. Both DJ-1- and glyoxalase-deficient cells display 4-fold increases in protein glycation levels, especially in unstressed cells |
740002 |
3.5.1.124 | malfunction |
reduced DJ-1 activity due to mutations or oxidative stress may lead to the accumulation of glycated alpha-synuclein and its aggregates |
753645 |