Cloned (Comment) | Organism |
---|---|
gene pepQ, recombinant expression of His-tagged enzyme | Xanthomonas campestris pv. campestris |
Crystallization (Comment) | Organism |
---|---|
purified recombinant detagged isozyme XPD43 by microbatch-under-oil technique, mixing of 0.002 ml of 12 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml of crystallization solution containing 40 mM KH2PO4, 15% glycerol, and 12% PEG 8000, 45 days, 21°C, X-ray diffraction structure determination and analysis by 1.83 A resolution | Xanthomonas campestris pv. campestris |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
70000 | - |
recombinant enzyme, gel filtration | Xanthomonas campestris pv. campestris |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xanthomonas campestris pv. campestris | Q8P839 | - |
- |
Xanthomonas campestris pv. campestris ATCC 33913 | Q8P839 | - |
- |
Xanthomonas campestris pv. campestris DSM 3586 | Q8P839 | - |
- |
Xanthomonas campestris pv. campestris LMG 568 | Q8P839 | - |
- |
Xanthomonas campestris pv. campestris NCPPB 528 | Q8P839 | - |
- |
Xanthomonas campestris pv. campestris P 25 | Q8P839 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme by nickel affinity chromatography, dialysis, tag cleavage by TEV protease, again affinity chromatography, ultrafiltration, and gel filtration | Xanthomonas campestris pv. campestris |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus | Xanthomonas campestris pv. campestris | ? | - |
? | |
additional information | Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus | Xanthomonas campestris pv. campestris P 25 | ? | - |
? | |
additional information | Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus | Xanthomonas campestris pv. campestris NCPPB 528 | ? | - |
? | |
additional information | Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus | Xanthomonas campestris pv. campestris LMG 568 | ? | - |
? | |
additional information | Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus | Xanthomonas campestris pv. campestris ATCC 33913 | ? | - |
? | |
additional information | Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus | Xanthomonas campestris pv. campestris DSM 3586 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 42800, about, sequence calculation | Xanthomonas campestris pv. campestris |
Synonyms | Comment | Organism |
---|---|---|
PepQ | - |
Xanthomonas campestris pv. campestris |
peptidase-Q | - |
Xanthomonas campestris pv. campestris |
prolidase | - |
Xanthomonas campestris pv. campestris |
XPD | - |
Xanthomonas campestris pv. campestris |
XPD43 | - |
Xanthomonas campestris pv. campestris |
General Information | Comment | Organism |
---|---|---|
evolution | XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea | Xanthomonas campestris pv. campestris |
physiological function | isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family | Xanthomonas campestris pv. campestris |