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Literature summary for 3.4.13.9 extracted from

  • Kumar, A.; Are, V.N.; Ghosh, B.; Agrawal, U.; Jamdar, S.N.; Makde, R.D.; Sharma, S.M.
    Crystallization and preliminary X-ray diffraction analysis of Xaa-Pro dipeptidase from Xanthomonas campestris (2014), Acta Crystallogr. Sect. F, 70, 1268-1271.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene pepQ, recombinant expression of His-tagged enzyme Xanthomonas campestris pv. campestris

Crystallization (Commentary)

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 [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
recombinant enzyme, gel filtration Xanthomonas campestris pv. campestris

Organism

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 (Commentary)

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 and Products (Substrate)

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

Subunits Comment Organism
dimer 2 * 42800, about, sequence calculation Xanthomonas campestris pv. campestris

Synonyms

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

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