Cloned (Comment) | Organism |
---|---|
gene argX, sequence comparisons and phylogenetic analysis | Sulfolobus acidocaldarius |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme in complex with ADP and with substrate StLysW, X-ray diffraction structure determination and analysis at 1.8 A resolution | Sulfolobus acidocaldarius |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Sulfolobus acidocaldarius | |
additional information | LysW contains an N-terminally bound Zn2+ | Sulfolobus acidocaldarius | |
sulfate | enzyme bound, the sulfate ion is replaced with the phosphate moiety of acylphosphate intermediate of StLysW in the structure model | Sulfolobus acidocaldarius |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | Sulfolobus acidocaldarius | - |
ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | Sulfolobus acidocaldarius DSM 639 | - |
ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | Sulfolobus acidocaldarius ATCC 33909 | - |
ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | Sulfolobus acidocaldarius NBRC 15157 | - |
ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | Sulfolobus acidocaldarius NCIMB 11770 | - |
ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | Sulfolobus acidocaldarius JCM 8929 | - |
ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus acidocaldarius | Q4J8E7 | - |
- |
Sulfolobus acidocaldarius ATCC 33909 | Q4J8E7 | - |
- |
Sulfolobus acidocaldarius DSM 639 | Q4J8E7 | - |
- |
Sulfolobus acidocaldarius JCM 8929 | Q4J8E7 | - |
- |
Sulfolobus acidocaldarius NBRC 15157 | Q4J8E7 | - |
- |
Sulfolobus acidocaldarius NCIMB 11770 | Q4J8E7 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | - |
Sulfolobus acidocaldarius | ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | - |
Sulfolobus acidocaldarius DSM 639 | ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | - |
Sulfolobus acidocaldarius ATCC 33909 | ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | - |
Sulfolobus acidocaldarius NBRC 15157 | ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | - |
Sulfolobus acidocaldarius NCIMB 11770 | ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? | |
ATP + L-glutamate + [LysW]-C-terminal-L-glutamate | - |
Sulfolobus acidocaldarius JCM 8929 | ADP + phosphate + [LysW]-C-terminal-gamma-(L-glutamyl)-L-glutamate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ArgX | - |
Sulfolobus acidocaldarius |
More | cf. EC 6.3.2.43 | Sulfolobus acidocaldarius |
StArgX | - |
Sulfolobus acidocaldarius |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Sulfolobus acidocaldarius |
General Information | Comment | Organism |
---|---|---|
evolution | gene duplication events at different stages of evolution led to ArgX and LysX (EC 6.3.2.43) | Sulfolobus acidocaldarius |
metabolism | lysine and arginine biosyntheses are mediated by a common carrier protein in Sulfolobus acidocaldarius. In this archaeon, after LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions | Sulfolobus acidocaldarius |
additional information | StArgX/ADP structrue analysis, and structure of substrate StLysW and recognition by enzyme StArgX, structural model of the phosphoryl intermediate in the StArgX reaction, overview. The alpha-amino group of the substrate glutmate molecule is to be ligated with the gamma-carboxyl group of Glu56 residue of StLysW. Interaction analysis of ArgX and LysW | Sulfolobus acidocaldarius |
physiological function | the hyperthermophilic archaeon Sulfolobus acidocaldarius not only biosynthesizes lysine through LysW-mediated protection of alpha-aminoadipate (AAA), but also uses the amino-group carrier protein LysW to protect the amino group of glutamate in arginine biosynthesis, cf. EC 6.3.2.43. ArgX is the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW | Sulfolobus acidocaldarius |