Recombinant E. coli hchA protein
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Recombinant E. coli hchA protein is a Escherichia coli K-12 Full Length protein, in the 1 to 283 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
yedU, yzzC, b1967, JW1950, hchA, Protein/nucleic acid deglycase 1, Glyoxalase III, Holding molecular chaperone, Hsp31, Maillard deglycase
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant E. coli hchA protein (AB106879)
15% SDS-PAGE analysis of 3 μg ab106879.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
This enzyme facilitates key reactions by dephosphorylating substrates impacting metabolism regulation. It may associate with other proteins to form complexes that contribute to cellular processes. hchA directly affects cellular maintenance by regulating levels of phosphorylated molecules important for proper cellular function and homeostasis.
Pathways
This target engages in metabolic pathways essential for cellular energy and repair processes. hchA interacts with pathways involving glucose metabolism where it collaborates with enzymes such as fructose-16-bisphosphatase. Furthermore it contributes to nucleotide biosynthesis pathways requiring cooperation with other hydrolases to ensure the proper balance of nucleotides within the cell.
Specifications
Form
Liquid
Additional notes
ab106879 was purified using conventional chromatography techniques.
General info
Function
Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals (PubMed : 26102038, PubMed : 26774339, PubMed : 28596309). Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) that cause irreversible damage (PubMed : 26102038, PubMed : 26774339). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (PubMed : 28596309). Has been reported to display chaperone, peptidase and glutathione-independent glyoxalase activities (PubMed : 12235139, PubMed : 12565879, PubMed : 14731284, PubMed : 15550391, PubMed : 21696459, PubMed : 7848303). However, these apparently disparate activities are all recruited to execute its protein deglycase primary function (PubMed : 26102038, PubMed : 26774339). Plays an important role in protecting cells from carbonyl stress, severe heat shock and starvation, as well as in acid resistance of stationary-phase cells (PubMed : 12235139, PubMed : 16796689, PubMed : 17158627).
Sequence similarities
Belongs to the peptidase C56 family. HchA subfamily.
Target data
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