| Product Name | gldA, 1-367aa (Bioactivity Validated) |
|---|---|
| Description | gldA catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). This protein allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. gldA possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively. Recombinant E. coli gldA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | Glycerol dehydrogenase, ECK3937, JW5556 |
| Host | E. coli |
| Molecular Weight |
95.6kDa (863aa) (100-150kDa in SDS-PAGE under reducing conditions.) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMDRIIQS PGKYIQGADV INRLGEYLKP LAERWLVVGD KFVLGFAQST VEKSFKDAGL VVEIAPFGGE CSQNEIDRLR GIAETAQCGA ILGIGGGKTL DTAKALAHFM GVPVAIAPTI ASTDAPCSAL SVIYTDEGEF DRYLLLPNNP NMVIVDTKIV AGAPARLLAA GIGDALATWF EARACSRSGA TTMAGGKCTQ AALALAELCY NTLLEEGEKA MLAAEQHVVT PALERVIEAN TYLSGVGFES GGLAAAHAVH NGLTAIPDAH HYYHGEKVAF GTLTQLVLEN APVEEIETVA ALSHAVGLPI TLAQLDIKED VPAKMRIVAE AACAEGETIH NMPGGATPDQ VYAALLVADQ YGQRFLQEWE |
| Tag | His-tag |
| Reactivity | E. coli |
| Applications | SDS-PAGE |
| Form | Liquid, in phosphate buffered saline (pH7.4) containing 10% glycerol. |
| Concentration | 0.25mg/ml (determined by absorbance at 280nm) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Subedi K.P., et al. (2008) FEMS Microbiol. Lett. 279:180-187 Gonzalez R., et al. (2008) Metab. Eng. 10:234-245 |
| Background | gldA catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). This protein allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. gldA possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively. Recombinant E. coli gldA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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