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2-imidazolidone-4-carboxylate + ATP + H2O
2-imidazolidone + ADP + phosphate
2-imidazoline-4-carboxylate + ATP + H2O
2-imidazoline-4-carboxylate + ADP + phosphate
-
does not undergo ring cleavage, but stimulates formation of inorganic phosphate from ATP
-
-
?
2-imidazolinone-4-carboxylate + H2O
?
-
-
-
-
?
2-oxo-5,5-dimethylthiazolidine-4-carboxylate + H2O
?
-
-
-
-
?
2-piperidone-6-carboxylate + ATP + H2O
2-aminoadipate + phosphate + ADP
2-thiazolinone-4-carboxylate + H2O
?
-
-
-
-
?
3-methyl-5-oxoproline + H2O
2-amino-3-methylpentanedioic acid
-
-
-
-
?
3-oxy-5-oxoproline + H2O
3-oxyglutamate + phosphate
4-methyl-5-oxoproline + H2O
2-amino-4-methylpentanedioic acid
-
-
-
-
?
4-oxy-5-oxoproline + H2O
4-oxyglutamate + phosphate
5'-p-fluorosulfonylbenzoyladenosine + H2O
?
-
-
-
-
?
5'-p-fluorosulfonylbenzoylinosine + H2O
?
-
-
-
-
?
5-oxo-L-proline + ATP + 2 H2O
L-glutamate + phosphate + ADP
-
assay at pH 7.2, 5 mM substrate, 4°C, 20 min
-
-
?
5-oxo-L-proline + ATP + H2O
L-glutamate + ADP + phosphate
assay at 30°C, pH 9.5, reaction stopped by 20 microl acetic acid and heating for 5 min at 100°C
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
alpha-hydroxyglutarate lactone + H2O
?
-
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
DL-2-oxo-3,3-dimethylthiazolidine-4-carboxylate + H2O
?
-
-
-
-
?
DL-cis-2-oxo-5-methyloxazolidine-4-carboxylate + H2O
DL-threonine + ADP + phosphate
-
-
-
-
?
L-2-iminothiazolidine-4-carboxylate + H2O
L-cystine
-
-
-
-
?
L-2-oxooxazolidine-4-carboxylate + H2O + ATP
L-serine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
L-2-oxothiazolidine-4-carboxylic acid + H2O
L-cysteine + ADP + phosphate
L-dihydroorotate + H2O
?
-
do not undergo ring cleavage, but stimulates formation of inorganic phosphate from ATP
-
-
?
L-trans-2-oxo-5-methyloxazolidine-4-carboxylate + H2O
L-threonine + ADP + phosphate
-
-
-
-
?
XTP + H2O
?
-
less than 5% of the activity observed with ATP
-
-
?
additional information
?
-
2-imidazolidone-4-carboxylate + ATP + H2O
2-imidazolidone + ADP + phosphate
-
-
-
-
?
2-imidazolidone-4-carboxylate + ATP + H2O
2-imidazolidone + ADP + phosphate
-
promotes enzymatic hydrolysis of ATP but is not itself hydrolyzed
-
-
?
2-piperidone-6-carboxylate + ATP + H2O
2-aminoadipate + phosphate + ADP
-
-
-
-
?
2-piperidone-6-carboxylate + ATP + H2O
2-aminoadipate + phosphate + ADP
-
-
-
?
3-oxy-5-oxoproline + H2O
3-oxyglutamate + phosphate
-
-
-
-
?
3-oxy-5-oxoproline + H2O
3-oxyglutamate + phosphate
-
-
-
?
4-oxy-5-oxoproline + H2O
4-oxyglutamate + phosphate
-
-
-
-
?
4-oxy-5-oxoproline + H2O
4-oxyglutamate + phosphate
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
component F8 + component beta5
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
209370, 209371, 209373, 209374, 209375, 209376, 209377, 209378, 209379, 209380, 209381, 209382, 209383, 209384, 209385, 209386, 209387, 209390, 209393, 209394 -
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
ir
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
conversion essentially irreversible, very slow reversal can be shown by measurement of ATP formation in presence of high glutamate concentrations
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
conversion essentially irreversible, very slow reversal can be shown by measurement of ATP formation in presence of high glutamate concentrations
-
-
ir
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
ATP is required
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
ATP in form of MnATP2-
-
-
?
ATP + H2O
?
-
-
-
-
?
CTP + H2O
?
-
less than 5% of the activity observed with ATP
-
-
?
CTP + H2O
?
-
less than 5% of the activity observed with ATP
-
-
?
dATP + H2O
?
-
-
-
-
?
GTP + H2O
?
-
less than 5% of the activity observed with ATP
-
-
?
GTP + H2O
?
-
less than 5% of the activity observed with ATP
-
-
?
ITP + H2O
?
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylate + H2O + ATP
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylic acid + H2O
L-cysteine + ADP + phosphate
-
-
-
-
?
L-2-oxothiazolidine-4-carboxylic acid + H2O
L-cysteine + ADP + phosphate
-
-
-
-
?
MgATP2- + H2O
?
-
-
-
-
?
MgATP2- + H2O
?
-
component beta5
-
-
?
MgATP2- + H2O
?
-
-
-
-
?
MgATP2- + H2O
?
-
-
-
-
?
UTP + H2O
?
-
less than 5% of the activity observed with ATP
-
-
?
UTP + H2O
?
-
less than 5% of the activity observed with ATP
-
-
?
additional information
?
-
-
CTP, TTP and UTP are no substrates
-
-
?
additional information
?
-
-
CTP, TTP and UTP are no substrates
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no activity observed with 5-oxo-D-proline
-
-
?
additional information
?
-
-
no activity observed with 5-oxo-D-proline
-
-
?
additional information
?
-
-
no activity observed with 5-oxo-D-proline
-
-
?
additional information
?
-
-
L-thioproline is no substrate
-
-
?
additional information
?
-
-
5-oxo-D-proline, 2-pyrrolidone-4-carboxylate, N-methyl-5-oxo-L-proline and N-acetyl-L-alanine are no substrates
-
-
?
additional information
?
-
-
L-proline, 2-pyrrolidone, N-methyl-5-oxo-L-proline, DL-piperidine-2-carboxylic acid and cyclohexanone-3-carboxylic acid are no substrates
-
-
?
additional information
?
-
-
L-proline, 2-pyrrolidone, N-methyl-5-oxo-L-proline, DL-piperidine-2-carboxylic acid and cyclohexanone-3-carboxylic acid are no substrates
-
-
?
additional information
?
-
-
CTP and UTP are poor substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
209370, 209373, 209375, 209376, 209378, 209379, 209380, 209381, 209382, 209383, 209384, 209385, 209386, 209387, 209390, 209393, 209394 -
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
conversion essentially irreversible, very slow reversal can be shown by measurement of ATP formation in presence of high glutamate concentrations
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
conversion essentially irreversible, very slow reversal can be shown by measurement of ATP formation in presence of high glutamate concentrations
-
-
ir
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
5-oxo-L-proline + H2O + ATP
L-glutamate + ADP + phosphate
-
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
ATP + 5-oxo-L-proline + 2 H2O
ADP + phosphate + L-glutamate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-oxoprolinase (atp-hydrolysing) deficiency
5-Oxoprolinase deficiency associated with severe psychomotor developmental delay, failure to thrive, microcephaly and microcytic anaemia.
5-oxoprolinase (atp-hydrolysing) deficiency
5-Oxoprolinase deficiency: report of the first human OPLAH mutation.
5-oxoprolinase (atp-hydrolysing) deficiency
5-Oxoprolinuria associated with 5-oxoprolinase deficiency; further evidence that this is a benign disorder.
5-oxoprolinase (atp-hydrolysing) deficiency
5-oxoprolinuria due to hereditary 5-oxoprolinase deficiency in two brothers--a new inborn error of the gamma-glutamyl cycle.
5-oxoprolinase (atp-hydrolysing) deficiency
5-Oxoprolinuria in Heterozygous Patients for 5-Oxoprolinase (OPLAH) Missense Changes.
5-oxoprolinase (atp-hydrolysing) deficiency
5-Oxoprolinuria in patients with and without defects in the gamma-glutamyl cycle.
5-oxoprolinase (atp-hydrolysing) deficiency
A newborn infant with generalized glutathione synthetase deficiency.
5-oxoprolinase (atp-hydrolysing) deficiency
Acetaminophen Use Concomitant with Long-Lasting Flucloxacillin Therapy: A Dangerous Combination.
5-oxoprolinase (atp-hydrolysing) deficiency
Clinical, biochemical, and molecular characterization of patients with glutathione synthetase deficiency.
5-oxoprolinase (atp-hydrolysing) deficiency
Coma, metabolic acidosis, and methemoglobinemia in a patient with acetaminophen toxicity.
5-oxoprolinase (atp-hydrolysing) deficiency
Five Chinese patients with 5-oxoprolinuria due to glutathione synthetase and 5-oxoprolinase deficiencies.
5-oxoprolinase (atp-hydrolysing) deficiency
Growth failure, encephalopathy, and endocrine dysfunctions in two siblings, one with 5-oxoprolinase deficiency.
5-oxoprolinase (atp-hydrolysing) deficiency
Inborn errors in the metabolism of glutathione.
5-oxoprolinase (atp-hydrolysing) deficiency
New insights into the genetics of 5-oxoprolinase deficiency and further evidence that it is a benign biochemical condition.
5-oxoprolinase (atp-hydrolysing) deficiency
Patients with genetic defects in the gamma-glutamyl cycle.
5-oxoprolinase (atp-hydrolysing) deficiency
Pyroglutamic acid-induced metabolic acidosis: a case report.
5-oxoprolinase (atp-hydrolysing) deficiency
Unravelling 5-oxoprolinuria (pyroglutamic aciduria) due to bi-allelic OPLAH mutations: 20 new mutations in 14 families.
5-oxoprolinase (atp-hydrolysing) deficiency
[5-Oxoprolinase deficiency]
Acidosis
Transient 5-oxoprolinuria (pyroglutamic aciduria) with systemic acidosis in an adult receiving antibiotic therapy.
Anemia
5-Oxoprolinase deficiency associated with severe psychomotor developmental delay, failure to thrive, microcephaly and microcytic anaemia.
Anemia, Hemolytic
Patients with genetic defects in the gamma-glutamyl cycle.
Anemia, Hemolytic
Unravelling 5-oxoprolinuria (pyroglutamic aciduria) due to bi-allelic OPLAH mutations: 20 new mutations in 14 families.
Brain Diseases
Growth failure, encephalopathy, and endocrine dysfunctions in two siblings, one with 5-oxoprolinase deficiency.
Breast Neoplasms
Glutamine affects glutathione recycling enzymes in a DMBA-induced breast cancer model.
Drug-Related Side Effects and Adverse Reactions
Potential for selective modulation of glutathione in cancer chemotherapy.
gamma-glutamyltransferase deficiency
Patients with genetic defects in the gamma-glutamyl cycle.
glutathione synthase deficiency
5-Oxoprolinuria in patients with and without defects in the gamma-glutamyl cycle.
glutathione synthase deficiency
A newborn infant with generalized glutathione synthetase deficiency.
glutathione synthase deficiency
Clinical, biochemical, and molecular characterization of patients with glutathione synthetase deficiency.
glutathione synthase deficiency
Patients with genetic defects in the gamma-glutamyl cycle.
glutathione synthase deficiency
Pyroglutamic aciduria (5-oxoprolinuria) without glutathione synthetase deficiency and with decreased pyroglutamate hydrolase activity.
glutathione synthase deficiency
Unravelling 5-oxoprolinuria (pyroglutamic aciduria) due to bi-allelic OPLAH mutations: 20 new mutations in 14 families.
Heart Failure
Heart failure and the glutathione cycle: an integrated view.
Heart Failure
OPLAH ablation leads to accumulation of 5-oxoproline, oxidative stress, fibrosis, and elevated fillings pressures: a murine model for heart failure with a preserved ejection fraction.
Malnutrition
Acetaminophen Use Concomitant with Long-Lasting Flucloxacillin Therapy: A Dangerous Combination.
Malnutrition
Pyroglutamic acid-induced metabolic acidosis: a case report.
membrane alanyl aminopeptidase deficiency
Inborn errors in the metabolism of glutathione.
Microcephaly
5-Oxoprolinase deficiency associated with severe psychomotor developmental delay, failure to thrive, microcephaly and microcytic anaemia.
Neoplasms
Activity and distribution of the cysteine prodrug activating enzyme, 5-oxo-L-prolinase, in human normal and tumor tissues.
Neoplasms
Characterization of 5-oxo-L-prolinase in normal and tumor tissues of humans and rats: a potential new target for biochemical modulation of glutathione.
Neoplasms
Glutamine affects glutathione recycling enzymes in a DMBA-induced breast cancer model.
Neoplasms
Increased expression of the MGMT repair protein mediated by cysteine prodrugs and chemopreventative natural products in human lymphocytes and tumor cell lines.
Neoplasms
Modulation of glutathione by a cysteine pro-drug enhances in vivo tumor response.
Neoplasms
Novel methylated DNA markers accurately discriminate Lynch syndrome associated colorectal neoplasia.
Neoplasms
Selective glutathione repletion with oral oxothiazolidine carboxylate (OTZ) in the radiated tumor-bearing rat.
Neoplasms
Sensitization effect of L-2-oxothiazolidine-4-carboxylate on tumor cells to melphalan and the role of 5-oxo-L-prolinase in glutathione modulation in tumor cells.
Sepsis
Acetaminophen Use Concomitant with Long-Lasting Flucloxacillin Therapy: A Dangerous Combination.
Sepsis
Pyroglutamic acid-induced metabolic acidosis: a case report.
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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
evolution
detailed phylogenetic analysis of 5-oxoprolinases, overview
evolution
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
evolution
-
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
-
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
-
evolution
-
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
-
evolution
-
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
-
evolution
-
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
-
evolution
-
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
-
evolution
-
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
-
evolution
-
detailed phylogenetic analysis of 5-oxoprolinases, overview
-
evolution
-
phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization
-
malfunction
inherited 5-oxoprolinase deficiency is a rare 5-oxoprolinase deficiency is an extremely rare disorder of the gamma-glutamyl cycle characterised by 5-oxoprolinuria, heterogeneity of the clinical presentation which ranges from normal to significant neurological involvement, genotype-phenotype correlation, phenotypes, overview
malfunction
inherited 5-oxoprolinase deficiency is a rare inborn condition characterised by 5-oxoprolinuria. Three enzyme mutations are involved: p.H870Pfs in a homozygous state, which results in a truncated protein, and two heterozygous missense changes, S323R and V1089I
malfunction
5-oxo-L-proline is a competitive inhibitor for glutamate transport in Sulfolobus solfataricus. The growth inhibiting effect of 5-oxo-L-proline on the cell culture is not only due to the loss of available carbon, because its addition to a growing culture can lead to cell death
malfunction
deletion of FgOXP1 or FgOXP2 in Fusarium graminearum leads to significant defects in its virulence on wheat, likely caused by an observed decreased deoxynivalenol (DON, a mycotoxin) production in the gene deletion mutant strains. DON is one of the best characterized virulence factors of Fusarium graminearum. The FgOXP2 deletion mutant strains are also defective in conidiation and sexual reproduction while the FgOXP1 deletion mutant strains are normal for those phenotypes. Double deletion of FgOXP1 and FgOXP2 leads to more severe defects in conidiation, DON production and virulence on plants, suggesting that both FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. Although transformation of the enzyme from Magnaporthe oryzae wild-type strain 70-15, MoOXP1, into DELTAFgoxp1 is able to complement DELTAFgoxp1, transformation of MoOXP1 into DELTAFgoxp2 fails to restore its defects in sexual development, DON production, and pathogenicity. Defects noticed in the gene deletion mutant strains of 5-oxoprolinase in Fusarium graminearum are caused by the affected gamma-glutamyl cycle, phenotypes, overview
malfunction
deletion of FgOXP1 or FgOXP2 in Fusarium graminearum leads to significant defects in its virulence on wheat, likely caused by an observed decreased deoxynivalenol (DON, a mycotoxin) production in the gene deletion mutant strains. DON is one of the best characterized virulence factors of Fusarium graminearum. The FgOXP2 deletion mutant strains are also defective in conidiation and sexual reproduction while the FgOXP1 deletion mutant strains are normal for those phenotypes. Double deletion of FgOXP1 and FgOXP2 leads to more severe defects in conidiation, DON production and virulence on plants, suggesting that both FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. Although transformation of the enzyme from Magnaporthe oryzae wild-type strain 70-15, MoOXP1, into DELTAFgoxp1, transformation of MoOXP1 into DELTAFgoxp2 fails to restore its defects in sexual development, DON production, and pathogenicity. Defects noticed in the gene deletion mutant strains of 5-oxoprolinase in Fusarium graminearum are caused by the affected gamma-glutamyl cycle, phenotypes, overview
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
malfunction
-
5-oxo-L-proline is a competitive inhibitor for glutamate transport in Sulfolobus solfataricus. The growth inhibiting effect of 5-oxo-L-proline on the cell culture is not only due to the loss of available carbon, because its addition to a growing culture can lead to cell death
-
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
-
malfunction
-
5-oxo-L-proline is a competitive inhibitor for glutamate transport in Sulfolobus solfataricus. The growth inhibiting effect of 5-oxo-L-proline on the cell culture is not only due to the loss of available carbon, because its addition to a growing culture can lead to cell death
-
malfunction
-
5-oxo-L-proline is a competitive inhibitor for glutamate transport in Sulfolobus solfataricus. The growth inhibiting effect of 5-oxo-L-proline on the cell culture is not only due to the loss of available carbon, because its addition to a growing culture can lead to cell death
-
malfunction
-
5-oxo-L-proline is a competitive inhibitor for glutamate transport in Sulfolobus solfataricus. The growth inhibiting effect of 5-oxo-L-proline on the cell culture is not only due to the loss of available carbon, because its addition to a growing culture can lead to cell death
-
malfunction
-
deletion of FgOXP1 or FgOXP2 in Fusarium graminearum leads to significant defects in its virulence on wheat, likely caused by an observed decreased deoxynivalenol (DON, a mycotoxin) production in the gene deletion mutant strains. DON is one of the best characterized virulence factors of Fusarium graminearum. The FgOXP2 deletion mutant strains are also defective in conidiation and sexual reproduction while the FgOXP1 deletion mutant strains are normal for those phenotypes. Double deletion of FgOXP1 and FgOXP2 leads to more severe defects in conidiation, DON production and virulence on plants, suggesting that both FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. Although transformation of the enzyme from Magnaporthe oryzae wild-type strain 70-15, MoOXP1, into DELTAFgoxp1, transformation of MoOXP1 into DELTAFgoxp2 fails to restore its defects in sexual development, DON production, and pathogenicity. Defects noticed in the gene deletion mutant strains of 5-oxoprolinase in Fusarium graminearum are caused by the affected gamma-glutamyl cycle, phenotypes, overview
-
malfunction
-
deletion of FgOXP1 or FgOXP2 in Fusarium graminearum leads to significant defects in its virulence on wheat, likely caused by an observed decreased deoxynivalenol (DON, a mycotoxin) production in the gene deletion mutant strains. DON is one of the best characterized virulence factors of Fusarium graminearum. The FgOXP2 deletion mutant strains are also defective in conidiation and sexual reproduction while the FgOXP1 deletion mutant strains are normal for those phenotypes. Double deletion of FgOXP1 and FgOXP2 leads to more severe defects in conidiation, DON production and virulence on plants, suggesting that both FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. Although transformation of the enzyme from Magnaporthe oryzae wild-type strain 70-15, MoOXP1, into DELTAFgoxp1 is able to complement DELTAFgoxp1, transformation of MoOXP1 into DELTAFgoxp2 fails to restore its defects in sexual development, DON production, and pathogenicity. Defects noticed in the gene deletion mutant strains of 5-oxoprolinase in Fusarium graminearum are caused by the affected gamma-glutamyl cycle, phenotypes, overview
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metabolism
the enzyme is involved in the gamma-glutamyl cycle, a six-enzyme cycle that represents the primary pathway for glutathione synthesis and degradation
metabolism
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
metabolism
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
metabolism
-
comparison of the effect of 5-oxoproline on the growth of Sulfolobus solfataricus and the closely related crenarchaeon Sulfolobus acidocaldarius. Sulfolobus solfataricus shows intracellular accumulation of 5-oxoproline and crude cell extract assays show a less effective degradation of 5-oxoproline. Sulfolobus acidocaldarius seems to be less versatile regarding carbohydrates and prefers peptidolytic growth compared to Sulfolobus solfataricus. Concludingly, Sulfolobus acidocaldarius exhibits a more efficient utilization of 5-oxoproline and is not inhibited by this compound, making it a better candidate for applications with glutamate-containing media at high temperatures
-
physiological function
comparison of the growth of 5-oxoprolinase deletion strains with wild-type strains in a variety of growth conditions does not yield any discernible phenotypes. Cells of glutamate auxotroph aco1D strain expressing OXP1 are able to grow on 5-oxoproline, although the growth is very slow
physiological function
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline to glutamate
physiological function
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline, i.e. pyroglutamate, to glutamate
physiological function
5-oxoprolinase is required for conidiation, sexual reproduction, virulence, and deoxynivalenol production of Fusarium graminearum. Both isozymes FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. FgOXP1 and FgOXP2 function differentially in deoxynivalenol DON production and in sexual reproduction of Fusarium graminearum, overview
physiological function
5-oxoprolinase is required for conidiation, sexual reproduction, virulence, and deoxynivalenol production of Fusarium graminearum. Both isozymes FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. FgOXP1 and FgOXP2 function differentially in deoxynivalenol DON production and in sexual reproduction of Fusarium graminearum, overview. A clearly much stronger role for Oxp2 in perithecia and ascus formation
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline, i.e. pyroglutamate, to glutamate
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline to glutamate
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline, i.e. pyroglutamate, to glutamate
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline, i.e. pyroglutamate, to glutamate
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline to glutamate
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline, i.e. pyroglutamate, to glutamate
-
physiological function
-
5-oxoprolinase is required for conidiation, sexual reproduction, virulence, and deoxynivalenol production of Fusarium graminearum. Both isozymes FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. FgOXP1 and FgOXP2 function differentially in deoxynivalenol DON production and in sexual reproduction of Fusarium graminearum, overview. A clearly much stronger role for Oxp2 in perithecia and ascus formation
-
physiological function
-
5-oxoprolinase is required for conidiation, sexual reproduction, virulence, and deoxynivalenol production of Fusarium graminearum. Both isozymes FgOXP1 and FgOXP2 play a role in fungal development and plant colonization. FgOXP1 and FgOXP2 function differentially in deoxynivalenol DON production and in sexual reproduction of Fusarium graminearum, overview
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline to glutamate
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline to glutamate
-
physiological function
-
5-oxoprolinase catalyses the ATP-dependent conversion of 5-oxoproline to glutamate
-
additional information
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to 5-oxoproline-induced growth restriction
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to 5-oxoproline-induced growth restriction
additional information
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to pyroglutamate-induced growth restriction
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to pyroglutamate-induced growth restriction
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
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
additional information
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
additional information
-
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to pyroglutamate-induced growth restriction
-
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
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to 5-oxoproline-induced growth restriction
-
additional information
-
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
-
additional information
-
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to pyroglutamate-induced growth restriction
-
additional information
-
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
-
additional information
-
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
-
additional information
-
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to pyroglutamate-induced growth restriction
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to 5-oxoproline-induced growth restriction
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to pyroglutamate-induced growth restriction
-
additional information
-
subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to 5-oxoproline-induced growth restriction
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to 5-oxoproline-induced growth restriction
-
additional information
-
glutamate is spontaneously converted into 5-oxoproline in a pH range of pH 2 to 3.5 and at temperatures above room temperature. This makes many thermoacidophiles, like, for example, Sulfolobus solfataricus, less suitable for a number of biotechnological approaches due to 5-oxoproline-induced growth restriction
-
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D1241V
naturally occuring mutation, leading to 5-oxoprolinase deficiency
G860R
naturally occuring mutation, leading to 5-oxoprolinase deficiency
S323R
naturally occuring mutation, leading to 5-oxoprolinase deficiency
V1089I
naturally occuring mutation, not involved into 5-oxoprolinase deficiency
additional information
oxp1-1 and oxp1-2, oxoprolinase knockout mutants
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
additional information
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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
additional information
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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
-
additional information
construction of isozyme FgOXP1 deletion mutant, DELTAFgoxp1, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
additional information
construction of isozyme FgOXP1 deletion mutant, DELTAFgoxp1, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
additional information
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construction of isozyme FgOXP1 deletion mutant, DELTAFgoxp1, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
additional information
construction of isozyme FgOXP2 deletion mutant, DELTAFgoxp2, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
additional information
construction of isozyme FgOXP2 deletion mutant, DELTAFgoxp2, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
additional information
-
construction of isozyme FgOXP2 deletion mutant, DELTAFgoxp2, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
additional information
-
construction of isozyme FgOXP2 deletion mutant, DELTAFgoxp2, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
-
additional information
-
construction of isozyme FgOXP1 deletion mutant, DELTAFgoxp1, and of double deletion mutant DELTAFgoxp1/Fgoxp2. Construction of GFP-tagged FgOXP1/2 complementary strains of Fusarium graminearum
-
additional information
in a yeast in vivo growth assay mutations S323R, G860R, and D1241V affect the activity of the enzyme
additional information
-
in a yeast in vivo growth assay mutations S323R, G860R, and D1241V affect the activity of the enzyme
additional information
subunit consists of two distinct domains HyuA and HyuB. Cells of a met15 deletion strain expressing either the HyuA or the HyuB domains alone cannot utilize 5-oxoproline sulfur analogue OTC as sole source of sulfur. Cells coexpressing both HyuA and HyuB domains are able to grow on OTC as a sole source of sulfur, similar to cells expressing full-length yeast 5-oxoprolinase gene
additional information
-
subunit consists of two distinct domains HyuA and HyuB. Cells of a met15 deletion strain expressing either the HyuA or the HyuB domains alone cannot utilize 5-oxoproline sulfur analogue OTC as sole source of sulfur. Cells coexpressing both HyuA and HyuB domains are able to grow on OTC as a sole source of sulfur, similar to cells expressing full-length yeast 5-oxoprolinase gene
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Metabolism in vivo of 5-oxo-L-proline and its inhibition by analogs of 5-oxo-L-proline
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Development of gamma-glutamylcysteine synthetase and oxoprolinase in rat kidney
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Enzymatic conversion of 5-oxo-L-proline (L-pyrrolidone carboxylate) to L-glutamate coupled with cleavage of adenosine triphosphate to adenosine diphosphate, a reaction in the gamma-glutamyl cycle
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292
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