Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.2.9 extracted from

  • Niehaus, T.D.; Elbadawi-Sidhu, M.; de Crecy-Lagard, V.; Fiehn, O.; Hanson, A.D.
    Discovery of a widespread prokaryotic 5-oxoprolinase that was hiding in plain sight (2017), J. Biol. Chem., 292, 16360-16367 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.2.9

Cloned(Commentary)

Cloned (Comment) Organism
genes pxpA, pxpB, and pxpC, comparative genomics, genetic structure, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged pxpA, and combined expression of N-terminally or C-terminally pxpB and pxpC, in Escherichia coli strain BL21(DE3) RIPL Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information inactivation of Bacillus subtilis pxpA, pxpB, or pxpC genes, deletion mutant phenotypes, overview. Mutant pxpABC deletants lack 5-oxoprolinase activity and accumulate 5-oxoproline. 5-Oxoprolinase activity can be reconstituted in vitro by mixing recombinant Bacillus subtilis PxpA, PxpB, and PxpC proteins Bacillus subtilis

General Stability

General Stability Organism
the activity of PxpABC is highly unstable Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 5-oxo-L-proline + 2 H2O Bacillus subtilis
-
 ADP + phosphate + L-glutamate
-
 ?
ATP + 5-oxo-L-proline + 2 H2O Bacillus subtilis 168
-
 ADP + phosphate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P42963 AND P60495 AND Q7WY77 subunits A, B, and C
-
Bacillus subtilis 168 P42963 AND P60495 AND Q7WY77 subunits A, B, and C
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme subunits from Escherichia coli strain BL21(DE3) RIPL by nickel affinity chromatography and desalting gel filtration Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5-oxo-L-proline + 2 H2O
-
 Bacillus subtilis ADP + phosphate + L-glutamate
-
 ?
ATP + 5-oxo-L-proline + 2 H2O
-
 Bacillus subtilis 168 ADP + phosphate + L-glutamate
-
 ?

Synonyms

Synonyms Comment Organism
ATP-dependent 5-oxoprolinase
-
 Bacillus subtilis
OPase
-
 Bacillus subtilis
prokaryotic 5-oxoprolinase
-
 Bacillus subtilis
PxpA gene name, encoding subunit A Bacillus subtilis
pxpB gene name, encoding subunit B Bacillus subtilis
pxpC gene name, encoding subunit C Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bacillus subtilis

General Information

General Information Comment Organism
evolution comparative analysis of prokaryotic genomes shows that the gene encoding pyroglutamyl peptidase, which removes N-terminal 5-oxoproline residues, clusters in diverse genomes with genes specifying homologs of a fungal lactamase (renamed prokaryotic 5-oxoprolinase A, pxpA) and homologs of allophanate hydrolase subunits (renamed pxpB and pxpC). 5-Oxoproline is a major universal metabolite damage product and its disposal systems are common in all domains of life Bacillus subtilis
malfunction inactivation of Bacillus subtilis pxpA, pxpB, or pxpC genes slows growth, causes 5-oxoproline accumulation in cells and medium, and prevents use of 5-oxoproline as a nitrogen source. ATP-dependent 5-oxoprolinase activity disappears when pxpA, pxpB, or pxpC is inactivated Bacillus subtilis
additional information neither PxpA nor PxpBC alone have detectable OPase activity, only combined in equimolar amounts, they show ATP-dependent OPase activity. The activity is highly unstable, kinetic constants cannot be determined Bacillus subtilis