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2-amino-4-phosphonobutyrate + 2-oxoglutarate
2-oxophosphonobutanoate + L-glutamate
-
-
-
-
r
2-amino-5-phosphonovalerate + 2-oxoglutarate
5-phosphono-2-oxopentanoate + L-glutamate
-
-
-
-
r
2-oxo-3-hydroxy-4-phosphobutanoate + L-glutamate
4-(phosphonooxy)-L-threonine + 2-oxoglutarate
-
2-oxo-3-hydroxy-4-phosphobutanoate = 3-hydroxy-4-O-phosphoryl-2-oxobutyrate
4-phospho-hydroxy-L-threonine = 4-O-phosphoryl-L-threonine
-
?
3-O-phospho-L-serine + 2-oxoglutarate
?
-
-
-
-
?
3-phosphonooxypyruvate + 2-oxoglutarate
?
-
-
-
-
?
3-phosphonooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
4-phosphooxy-L-threonine + 2-oxoglutarate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
homocysteate + 2-oxoglutarate
4-mercapto-2-oxobutanoate + L-glutamate
-
-
-
-
r
L-alanine + 3-phosphonooxypyruvate
O-phospho-L-serine + pyruvate
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
L-glutamate + 4,5-dioxopentanoate
5-aminolevulinate + 2-oxoglutarate
-
-
-
-
?
L-homoserine + 2-oxoglutarate
4-hydroxy-2-oxobutyrate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
additional information
?
-
3-phosphonooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
?
3-phosphonooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
?
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
4-phosphooxy-L-threonine + 2-oxoglutarate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
-
-
-
r
4-phosphooxy-L-threonine + 2-oxoglutarate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
-
-
-
r
L-alanine + 3-phosphonooxypyruvate
O-phospho-L-serine + pyruvate
-
-
-
-
r
L-alanine + 3-phosphonooxypyruvate
O-phospho-L-serine + pyruvate
-
L-alanine as amino group donor, 10% of the activity with L-glutamate
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
phosphorylated pathway for serine biosynthesis
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
forward reaction
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
phosphorylated pathway for serine biosynthesis
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
phosphorylated pathway for serine biosynthesis
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
phosphorylated pathway for serine biosynthesis
-
-
r
L-homoserine + 2-oxoglutarate
4-hydroxy-2-oxobutyrate + L-glutamate
L-homoserine transaminase reaction of engineered enzyme mutant R42W/R77W, low activity with the wild-type enzyme
-
-
r
L-homoserine + 2-oxoglutarate
4-hydroxy-2-oxobutyrate + L-glutamate
L-homoserine transaminase reaction of engineered enzyme mutant R42W/R77W, low activity with the wild-type enzyme
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
?
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
?
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
reverse reaction
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphonooxypyruvate + L-glutamate
-
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
additional information
?
-
the transamination reaction catalyzed by PSAT consists of two reversible half-reactions, overview. Substrate binding requires a conformational change of AtPSAT1
-
-
-
additional information
?
-
-
the transamination reaction catalyzed by PSAT consists of two reversible half-reactions, overview. Substrate binding requires a conformational change of AtPSAT1
-
-
-
additional information
?
-
the enzyme preferentially utilizes glutamate for transamination
-
-
-
additional information
?
-
the enzyme preferentially utilizes glutamate for transamination
-
-
-
additional information
?
-
-
the enzyme preferentially utilizes glutamate for transamination
-
-
-
additional information
?
-
the enzyme preferentially utilizes glutamate for transamination
-
-
-
additional information
?
-
the enzyme preferentially utilizes glutamate for transamination
-
-
-
additional information
?
-
-
2-amino-3-phosphonopropionate, 3-amino-3-phosphonopropionate 4-amino-4-phosphonobutyrate, 1-amino-1,3-phosphonopropane, 2-amino-6-phosphohexanoate, serine, aspartate, cysteine sulfinate and cysteate are no substrates
-
-
?
additional information
?
-
-
aspartate, alanine and phosphoserine as amino donors, 2-oxoglutarate and glyoxylate as amino acceptors
-
-
?
additional information
?
-
-
aspartate, alanine and phosphoserine as amino donors, 2-oxoglutarate and glyoxylate as amino acceptors
-
-
?
additional information
?
-
-
high aspartate aminotransferase side activity
-
-
?
additional information
?
-
-
hydroxypyruvate is unreactive
-
-
?
additional information
?
-
-
hydroxypyruvate is unreactive
-
-
?
additional information
?
-
-
4,5-dioxovalerate with glutamate as amino donor is effective as competitive substrate to phosphohydroxypyruvate in the forward reaction and yields 5-aminolevulinate, 4,5-dioxovalerate and glutamate-1-semialdehyde can both serve as competitive aminoacceptor in the reverse reaction with phosphoserine and as substrate with 2-oxoglutarate as aminoacceptor
-
-
?
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3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
4-phosphooxy-L-threonine + 2-oxoglutarate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
3-phosphooxypyruvate + L-glutamate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
4-phosphooxy-L-threonine + 2-oxoglutarate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
-
-
-
r
4-phosphooxy-L-threonine + 2-oxoglutarate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
phosphorylated pathway for serine biosynthesis
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
phosphorylated pathway for serine biosynthesis
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
-
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
phosphorylated pathway for serine biosynthesis
-
-
r
L-glutamate + 3-phosphohydroxypyruvate
O-phospho-L-serine + 2-oxoglutarate
-
phosphorylated pathway for serine biosynthesis
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
O-phospho-L-serine + 2-oxoglutarate
3-phosphooxypyruvate + L-glutamate
-
-
-
r
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.
Adenocarcinoma of Lung
Overexpression of PSAT1 promotes metastasis of lung adenocarcinoma by suppressing the IRF1-IFN? axis.
Adenocarcinoma, Mucinous
Proteomic characterization of ovarian cancers identifying annexin-A4, phosphoserine aminotransferase, cellular retinoic acid-binding protein 2, and serpin B5 as histology-specific biomarkers.
Brain Diseases
Two new cases of serine deficiency disorders treated with l-serine.
Breast Neoplasms
Association of DNA methylation of phosphoserine aminotransferase with response to endocrine therapy in patients with recurrent breast cancer.
Breast Neoplasms
Expression levels of serine/glycine metabolism-related proteins in triple negative breast cancer tissues.
Breast Neoplasms
Glutamine-utilizing transaminases are a metabolic vulnerability of TAZ/YAP-activated cancer cells.
Breast Neoplasms
Overexpression of the PSAT1 Gene in Nasopharyngeal Carcinoma Is an Indicator of Poor Prognosis.
Breast Neoplasms
Phosphoserine aminotransferase 1 is associated to poor outcome on tamoxifen therapy in recurrent breast cancer.
Breast Neoplasms
Selective loss of phosphoserine aminotransferase 1 (PSAT1) suppresses migration, invasion, and experimental metastasis in triple negative breast cancer.
Carcinogenesis
Overexpression of Phosphoserine Aminotransferase 1 (PSAT1) Predicts Poor Prognosis and Associates with Tumor Progression in Human Esophageal Squamous Cell Carcinoma.
Carcinoma
MicroRNA-365 suppresses cell growth and invasion in esophageal squamous cell carcinoma by modulating phosphoserine aminotransferase 1.
Carcinoma
Overexpression of Phosphoserine Aminotransferase 1 (PSAT1) Predicts Poor Prognosis and Associates with Tumor Progression in Human Esophageal Squamous Cell Carcinoma.
Carcinoma
Proteomic characterization of ovarian cancers identifying annexin-A4, phosphoserine aminotransferase, cellular retinoic acid-binding protein 2, and serpin B5 as histology-specific biomarkers.
Carcinoma, Non-Small-Cell Lung
Overexpression of the PSAT1 Gene in Nasopharyngeal Carcinoma Is an Indicator of Poor Prognosis.
Carcinoma, Non-Small-Cell Lung
PSAT1 regulates cyclin D1 degradation and sustains proliferation of non-small cell lung cancer cells.
Carcinoma, Ovarian Epithelial
PSAT1 Regulated Oxidation-Reduction Balance Affects the Growth and Prognosis of Epithelial Ovarian Cancer.
Colitis
GC-MS metabolomics on PPAR?-dependent exacerbation of colitis.
Colonic Neoplasms
Overexpression of phosphoserine aminotransferase PSAT1 stimulates cell growth and increases chemoresistance of colon cancer cells.
Colonic Neoplasms
Overexpression of the PSAT1 Gene in Nasopharyngeal Carcinoma Is an Indicator of Poor Prognosis.
Colorectal Neoplasms
Identification of differential proteins in colorectal cancer cells treated with caffeic acid phenethyl ester.
Colorectal Neoplasms
Overexpression of phosphoserine aminotransferase PSAT1 stimulates cell growth and increases chemoresistance of colon cancer cells.
Contracture
Adult diagnosis of congenital serine biosynthesis defect: A treatable cause of progressive neuropathy.
Cysts
[Enhancement of resistance of mice Toxoplasma gondii by 2 polysaccharides beta 1-3, beta 1-6 (PSAT and Scleroglucan)]
Drug-Related Side Effects and Adverse Reactions
Prolonged suppressive antibiotic therapy for prosthetic joint infection in the elderly: a national multicentre cohort study.
Epilepsy
Phosphoserine aminotransferase deficiency: imaging findings in a child with congenital microcephaly.
Esophageal Neoplasms
MicroRNA-340 Inhibits Esophageal Cancer Cell Growth and Invasion by Targeting Phosphoserine Aminotransferase 1.
Esophageal Neoplasms
MicroRNA-365 suppresses cell growth and invasion in esophageal squamous cell carcinoma by modulating phosphoserine aminotransferase 1.
Esophageal Squamous Cell Carcinoma
MicroRNA-365 suppresses cell growth and invasion in esophageal squamous cell carcinoma by modulating phosphoserine aminotransferase 1.
Esophageal Squamous Cell Carcinoma
Overexpression of Phosphoserine Aminotransferase 1 (PSAT1) Predicts Poor Prognosis and Associates with Tumor Progression in Human Esophageal Squamous Cell Carcinoma.
Glioblastoma
Regorafenib induces lethal autophagy arrest by stabilizing PSAT1 in glioblastoma.
Ichthyosis
Adult diagnosis of congenital serine biosynthesis defect: A treatable cause of progressive neuropathy.
Infections
Prolonged suppressive antibiotic therapy for prosthetic joint infection in the elderly: a national multicentre cohort study.
Infections
Subcutaneous suppressive antibiotic therapy for bone and joint infections: safety and outcome in a cohort of 10 patients.
Infections
[Enhancement of resistance of mice Toxoplasma gondii by 2 polysaccharides beta 1-3, beta 1-6 (PSAT and Scleroglucan)]
Insulin Resistance
Hepatic phosphoserine aminotransferase 1 (PSAT1) regulates insulin sensitivity in mice via tribbles homolog 3 (TRB3).
Intellectual Disability
On the phenotypic spectrum of serine biosynthesis defects.
Lung Neoplasms
Nuclear Pyruvate Kinase M2 (PKM2) Contributes to Phosphoserine Aminotransferase 1 (PSAT1)-Mediated Cell Migration in EGFR-Activated Lung Cancer Cells.
Lung Neoplasms
Overexpression of PSAT1 promotes metastasis of lung adenocarcinoma by suppressing the IRF1-IFN? axis.
Lung Neoplasms
Overexpression of the PSAT1 Gene in Nasopharyngeal Carcinoma Is an Indicator of Poor Prognosis.
Lung Neoplasms
PSAT1 regulates cyclin D1 degradation and sustains proliferation of non-small cell lung cancer cells.
Microcephaly
Phosphoserine aminotransferase deficiency: imaging findings in a child with congenital microcephaly.
Microcephaly
Two new cases of serine deficiency disorders treated with l-serine.
Neoplasm Metastasis
Long non-coding RNA RP4-694A7.2 Promotes Hepatocellular Carcinoma Cell Proliferation and Metastasis through the Regulation of PSAT1.
Neoplasm Metastasis
Selective loss of phosphoserine aminotransferase 1 (PSAT1) suppresses migration, invasion, and experimental metastasis in triple negative breast cancer.
Neoplasm Metastasis
[A comparaison between the total PSA, the Gleason score and the bone scintiscan results for different age groups]
Neoplasms
Artemether Exhibits Amoebicidal Activity against Acanthamoeba castellanii through Inhibition of the Serine Biosynthesis Pathway.
Neoplasms
Challenges and Opportunities in the Development of Serine Synthetic Pathway Inhibitors for Cancer Therapy.
Neoplasms
Knock-down of PSAT1 Enhances Sensitivity of NSCLC Cells to Glutamine-limiting Conditions.
Neoplasms
Nuclear Pyruvate Kinase M2 (PKM2) Contributes to Phosphoserine Aminotransferase 1 (PSAT1)-Mediated Cell Migration in EGFR-Activated Lung Cancer Cells.
Neoplasms
Overexpression of Phosphoserine Aminotransferase 1 (PSAT1) Predicts Poor Prognosis and Associates with Tumor Progression in Human Esophageal Squamous Cell Carcinoma.
Neoplasms
Prostate specific antigen (PSA) value adjusted for transition zone volume and free PSA (gamma-seminoprotein)/PSA ratio in the diagnosis of prostate cancer in patients with intermediate PSA levels.
Neoplasms
Proteomic and Mitochondrial Genomic Analyses of Pediatric Brain Tumors.
Neoplasms
Transition zone volume-adjusted prostate-specific antigen value predicts extracapsular carcinoma of the prostate in patients with intermediate prostate-specific antigen levels.
Neoplasms
Usefulness of Total PSA Value in Prostate Diseases Diagnosis.
Neoplasms
[Evaluation of (-2)proPSA in combination with total PSA and free PSA for the early detection of prostate cancer].
Neurodegenerative Diseases
Human Cerebral Cortex Proteome of Fragile X-Associated Tremor/Ataxia Syndrome.
Neurologic Manifestations
On the phenotypic spectrum of serine biosynthesis defects.
Obesity
Health disparities in clinical practice patterns for prostate cancer screening by geographic regions in the United States: a multilevel modeling analysis.
Ovarian Neoplasms
Proteomic characterization of ovarian cancers identifying annexin-A4, phosphoserine aminotransferase, cellular retinoic acid-binding protein 2, and serpin B5 as histology-specific biomarkers.
Pemphigoid, Bullous
Genetic basis of phenotypic plasticity for predator-induced morphological defenses in anuran tadpole, Rana pirica, using cDNA subtraction and microarray analysis.
phosphoserine transaminase deficiency
Adult diagnosis of congenital serine biosynthesis defect: A treatable cause of progressive neuropathy.
phosphoserine transaminase deficiency
Disturbed phospholipid metabolism in serine biosynthesis defects revealed by metabolomic profiling.
phosphoserine transaminase deficiency
Phosphoserine aminotransferase deficiency: a novel disorder of the serine biosynthesis pathway.
phosphoserine transaminase deficiency
Phosphoserine aminotransferase deficiency: imaging findings in a child with congenital microcephaly.
Phyllodes Tumor
Expression of serine and glycine-related enzymes in phyllodes tumor.
Precancerous Conditions
Usefulness of Total PSA Value in Prostate Diseases Diagnosis.
Prostatic Hyperplasia
Likelihood of prostate cancer based on prostate-specific antigen density by MRI: retrospective analysis.
Prostatic Hyperplasia
Usefulness of Total PSA Value in Prostate Diseases Diagnosis.
Prostatic Neoplasms
Health disparities in clinical practice patterns for prostate cancer screening by geographic regions in the United States: a multilevel modeling analysis.
Prostatic Neoplasms
Likelihood of prostate cancer based on prostate-specific antigen density by MRI: retrospective analysis.
Prostatic Neoplasms
Prostate specific antigen (PSA) value adjusted for transition zone volume and free PSA (gamma-seminoprotein)/PSA ratio in the diagnosis of prostate cancer in patients with intermediate PSA levels.
Prostatic Neoplasms
PSA value adjusted for the transition zone volume in the diagnosis of prostate cancer.
Prostatic Neoplasms
The influence of prostate volume on the prostate-specific antigen (PSA) level adjusted for the transition zone volume and free-to-total PSA ratio: a prospective study.
Prostatic Neoplasms
Usefulness of Total PSA Value in Prostate Diseases Diagnosis.
Prostatic Neoplasms
[A comparaison between the total PSA, the Gleason score and the bone scintiscan results for different age groups]
Prostatic Neoplasms
[Evaluation of (-2)proPSA in combination with total PSA and free PSA for the early detection of prostate cancer].
Prostatic Neoplasms
[Validity of PSA density of the transition zone in the diagnosis of prostate cancer]
Sepsis
Prolonged suppressive antibiotic therapy for prosthetic joint infection in the elderly: a national multicentre cohort study.
Triple Negative Breast Neoplasms
Expression levels of serine/glycine metabolism-related proteins in triple negative breast cancer tissues.
Triple Negative Breast Neoplasms
Selective loss of phosphoserine aminotransferase 1 (PSAT1) suppresses migration, invasion, and experimental metastasis in triple negative breast cancer.
Tuberculosis
Dysregulation of serine biosynthesis contributes to the growth defect of a Mycobacterium tuberculosis crp mutant.
Tuberculosis
Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis.
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0.007
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77W/H328E
0.01
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant H41K
0.022
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42E
0.031
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant H41Y
0.036
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77W/H328L
0.051
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant H41Q
0.058
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77E
0.079
substrate L-phosphoserine, pH 8.2, 30°C, recombinant mutant R42W/R77W
0.08
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77W/H328Y
0.115
substrate L-homoserine, pH 8.2, 30°C, recombinant wild-type enzyme
0.131
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42K
0.145
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R329G
0.148
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42Q
0.18
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77I
0.224
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77S
0.266
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W
0.273
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77T
0.281
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R329Q
0.293
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R329H
0.47
-
substrate: O-phospho-L-serine, pH 8.5, 25°C
0.487
substrate L-homoserine, pH 8.2, 30°C, recombinant mutant R42W/R77W
0.66
substrate: 2-oxoglutarate, pH 8.5, 25°C
0.67
substrate: O-phospho-L-serine, pH 8.5, 25°C
0.74
-
substrate: 2-oxoglutarate, pH 8.5, 25°C
1.3
purified enzyme, pH 8.1-8.2, 25°C
12
pH and temperature not specified in the publication
1416
purified enzyme, pH 6.8-7.2, 38°C
21.22
-
substrate: L-glutamate, pH 8.5, 25°C
3.406
pH 8.2, 30°C, substrate L-phosphoserine, recombinant wild-type enzyme
3.8
pH not specified in the publication, 25°C, purified recombinant enzyme, substrate 3-phosphooxypyruvate
42
purified recombinant enzyme, pH 6.1, 25°C
42.3
purified recombinant enzyme, pH 8.2, 25°C
44.4
purified recombinant enzyme mutant K2G, pH 6.1, 25°C
5.82
substrate: L-glutamate, pH 8.5, 25°C
6.14
substrate: 3-phosphohydroxypyruvate, pH 8.5, 25°C
7
purified enzyme, pH and temperature not specified in the publication
9.65
-
substrate: 3-phosphohydroxypyruvate, pH 8.5, 25°C
additional information
-
13 U/mg
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evolution
phosphoserine aminotransferases belong to the class IV of aminotransferases with the alpha-type fold. In general, this class of enzymes is characterized by the presence of two domains with mixed alpha/beta fold
evolution
the Arabidopsis genome contains three genes for the PGDH (At4g34200/PGDH1, At1g17745/ PGDH2, and At3g19480/ PGDH3), two genes for the PSAT (At4g35630/PSAT1, and At2g17630/PSAT2) and one gene for the PSP (At1g18640). The PSAT1 gene is the most expressed isoform in Arabidopsis thaliana
malfunction
a growth phenotype is observed for PSAT1-silenced plants due to serine deficiency
malfunction
a sericin-deficient silkworm strain exhibits a diminished expression of bmPSAT mRNA in the silk gland
malfunction
deletion of 45 N-terminal residues (EhPSAT_DELTA45) results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein
malfunction
-
a sericin-deficient silkworm strain exhibits a diminished expression of bmPSAT mRNA in the silk gland
-
malfunction
-
deletion of 45 N-terminal residues (EhPSAT_DELTA45) results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein
-
malfunction
-
a sericin-deficient silkworm strain exhibits a diminished expression of bmPSAT mRNA in the silk gland
-
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
metabolism
enzyme PSAT catalyses the second step of phosphorylated pathway of serine biosynthesis
metabolism
L-serine is involved in several important metabolic pathways in the protozoan parasite Entamoeba histolytica. Phosphoserine aminotransferase (PSAT) is a pyridoxal-5'phosphate (PLP)-dependent enzyme that catalyzes the second reversible step in the phosphoserine biosynthetic pathway producing L-serine
metabolism
phosphoserine aminotransferase (bmPSAT) from Bombyx mori is responsible for L-serine biosynthesis. This pathway composed of D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95), PSAT, and phosphoserine phosphatase (PSP, EC 3.1.3.3) is crucial for the de novo production of L-serine from a glycolytic intermediate, 3-phosphoglycerate
metabolism
phosphoserine aminotransferase (PSAT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the conversion of 3-phosphohydroxypyruvate (3-PHP) to 3-phosphoserine (PSer) in an L-glutamate (Glu)-linked reversible transamination reaction. This process in plants takes place in plastids. It is a part of the phosphorylated pathway of serine biosynthesis, one of three routes recognized in plant organisms that yield serine. In this three-step biotransformation, 3-phosphoglycerate (3-PGA) delivered from plastidial glycolysis and Calvin cycle is oxidized by 3-PGA dehydrogenase. Then, 3-PHP is subjected to transamination with Glu to yield PSer and 2-oxoglutarate (AKG). In the last step of the pathway, serine is produced by the action of phosphoserine phosphatase
metabolism
the serine biosynthesis pathway consists of three sequential reactions that are catalyzed by 3-phosphoglycerate dehydrogenase (PGDH), 3-phosphoserine aminotransferase (PSAT), and 3-phosphoserine phosphatase (PSP) enzymes, all localized in the plastids. Serine biosynthesis pathways in plants, overview
metabolism
transcriptional regulators TAZ and YAP (TAZ/YAP) promote glutamine dependence in breast cancer cells and activate the expression of glutamine-utilizing transaminases to support cell growth. TAZ and YAP induce glutamic-oxaloacetic transaminase (GOT1, EC 2.6.1.64) and phosphoserine aminotransferase (PSAT1) expression. Transcriptional regulators TAZ/YAP activity positively correlates with transaminase expression in breast cancer patients, while transaminase inhibitor aminooxyacetate (AOA) represses cell growth in a TAZ/YAP-dependent manner. Thus, transamination is a potential vulnerable metabolic requirement for TAZ/YAP-driven breast cancer
metabolism
-
phosphoserine aminotransferase (bmPSAT) from Bombyx mori is responsible for L-serine biosynthesis. This pathway composed of D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95), PSAT, and phosphoserine phosphatase (PSP, EC 3.1.3.3) is crucial for the de novo production of L-serine from a glycolytic intermediate, 3-phosphoglycerate
-
metabolism
-
L-serine is involved in several important metabolic pathways in the protozoan parasite Entamoeba histolytica. Phosphoserine aminotransferase (PSAT) is a pyridoxal-5'phosphate (PLP)-dependent enzyme that catalyzes the second reversible step in the phosphoserine biosynthetic pathway producing L-serine
-
metabolism
-
phosphoserine aminotransferase (bmPSAT) from Bombyx mori is responsible for L-serine biosynthesis. This pathway composed of D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95), PSAT, and phosphoserine phosphatase (PSP, EC 3.1.3.3) is crucial for the de novo production of L-serine from a glycolytic intermediate, 3-phosphoglycerate
-
physiological function
-
enzyme forms a protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry. Ionic interactions play a significant role in complex formation and stability. The nucleotide binding domain of D-phosphoglycerate dehydrogenase specifically interacts with the enzyme. The purified nucleotide binding domain of D-phosphoglycerate dehydrogenase interacts with phosphoserine transaminase. The reactions catalyzed by the complex suggest a possibility of substrate channelling in the protein complex
physiological function
enzyme is part of the phosphoserine pathway for serine synthesis. A model approach indicates a 3060% contribution of the phosphoserine pathway to the overall serine pool
physiological function
-
hepatic PSAT1 expression and liver serine levels are reduced in genetically engineered leptin receptor-deficient (db/db) mice and high-fat diet (HFD)-induced diabetic mice. Overexpression of PSAT1 by adenovirus expressing PSAT1 improves insulin signaling and insulin sensitivity in vitro and in vivo under normal conditions. Opposite effects are observed when PSAT1 is knocked down by small hairpin RNA specific for PSAT1. Overexpression of PSAT1 also significantly ameliorates insulin resistance in diabetic mice. PSAT1 inhibits the expression of hepatic tribbles homolog TRB3 in vitro and in vivo. Serine mediates PSAT1 regulation of TRB3 expression and insulin signaling in vitro
physiological function
analysis of association of PSAT1 protein levels upon tamoxifen treatment and enzyme role in tamoxifen resistance, PSAT1 protein and mRNA levels are significantly associated to poor outcome to tamoxifen treatment. Cytokine and JAK-STAT signaling are associated with PSAT1 expression. Clinical significance of PSAT1 in the gene expression cohort and pathway analysis
physiological function
phosphoserine aminotransferase (bmPSAT) from Bombyx mori is responsible for L-serine biosynthesis. bmPSAT may play an important role in synthesizing and supplying L-serine in the larva of Bombyx mori. The silk gland is the sole organ in which silk is synthesized and secreted in the silkworm. Silk is composed of two types of proteins: sericin and fibroin, both of which contain high levels of L-serine and glycine
physiological function
phosphoserine aminotransferase1 is part of the phosphorylated pathways for serine biosynthesis and essential for light and sugar-dependent growth promotion
physiological function
-
phosphoserine aminotransferase (bmPSAT) from Bombyx mori is responsible for L-serine biosynthesis. bmPSAT may play an important role in synthesizing and supplying L-serine in the larva of Bombyx mori. The silk gland is the sole organ in which silk is synthesized and secreted in the silkworm. Silk is composed of two types of proteins: sericin and fibroin, both of which contain high levels of L-serine and glycine
-
physiological function
-
phosphoserine aminotransferase (bmPSAT) from Bombyx mori is responsible for L-serine biosynthesis. bmPSAT may play an important role in synthesizing and supplying L-serine in the larva of Bombyx mori. The silk gland is the sole organ in which silk is synthesized and secreted in the silkworm. Silk is composed of two types of proteins: sericin and fibroin, both of which contain high levels of L-serine and glycine
-
additional information
conformational changes of the protein during the catalytic event concern (i) the neighborhood of K265 when the amino group is transferred to the cofactor to form PMP and (ii) movement of the gate-keeping loop (residues 391-401) upon binding of of 3-phosphohydroxypyruvate to 3-phosphoserine. The latter conformational change of the loop may likely be one of key elements that regulate catalytic activity of PSATs. The conserved catalytic lysine, which directly follows a hydrophobic beta-strand, is localized closer to the C-terminus than the Gly-rich region. PSATs have an aspartate residue which hydrogen bonds the pyridoxal ring N1 atom and precedes the Schiff base lysine by 20-50 amino acids. The complex structure with pyridoxamine shows the enzyme primes for a covalent binding of 3-phosphohydroxypyruvate. The complex structure with phopshoserine reveals the geminal diamine intermediate state
additional information
-
conformational changes of the protein during the catalytic event concern (i) the neighborhood of K265 when the amino group is transferred to the cofactor to form PMP and (ii) movement of the gate-keeping loop (residues 391-401) upon binding of of 3-phosphohydroxypyruvate to 3-phosphoserine. The latter conformational change of the loop may likely be one of key elements that regulate catalytic activity of PSATs. The conserved catalytic lysine, which directly follows a hydrophobic beta-strand, is localized closer to the C-terminus than the Gly-rich region. PSATs have an aspartate residue which hydrogen bonds the pyridoxal ring N1 atom and precedes the Schiff base lysine by 20-50 amino acids. The complex structure with pyridoxamine shows the enzyme primes for a covalent binding of 3-phosphohydroxypyruvate. The complex structure with phopshoserine reveals the geminal diamine intermediate state
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W101A
-
about 5% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. In mutant W101A, there are no big fluctuations but the stacking interaction is lost due to side chain truncation
W101F
-
about 70% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein
W101H
-
about 20% of wild-type activity, with very little global conformational change upon the mutation. An average minimum root mean square fluctuation per residue is observed for the wild-type protein as compared to mutants. The stacking interaction for mutants W101F and W101H are not as prominent as for the wild-type protein
H41K
site-directed mutagenesis
H41Q
site-directed mutagenesis
H41Y
site-directed mutagenesis
R42E
site-directed mutagenesis
R42K
site-directed mutagenesis
R42Q
site-directed mutagenesis
R42W
site-directed mutagenesis, the mutant exhibits high activity toward L-homoserine with a low activity toward L-phosphoserine
R42W/R329G
site-directed mutagenesis
R42W/R329H
site-directed mutagenesis
R42W/R329Q
site-directed mutagenesis
R42W/R77E
site-directed mutagenesis
R42W/R77I
site-directed mutagenesis
R42W/R77S
site-directed mutagenesis
R42W/R77T
site-directed mutagenesis
R42W/R77WH328E
site-directed mutagenesis, very low activity with L-homoserine
R42W/R77WH328K
site-directed mutagenesis, no activity with L-homoserine
R42W/R77WH328L
site-directed mutagenesis
R42W/R77WH328Y
site-directed mutagenesis
R42E
-
site-directed mutagenesis
-
R42K
-
site-directed mutagenesis
-
R42Q
-
site-directed mutagenesis
-
R42W/R77W
-
site-directed mutagenesis
-
K2G
site-directed mutagenesis
R42W/R77W
site-directed mutagenesis
R42W/R77W
site-directed mutagenesis, best engineered mutant showing 4.2fold increased activity with L-homoserine compared to wild-type enzyme, the activity toward the natural substrate L-phosphoserine is highly reduced in the mutant enzyme
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. Overexpression of the artificial PSAT1-silencing construct in Arabidopsis thaliana leads to a significant reduction of PSAT1 expression, which subsequently results in a strong inhibition of growth. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. Overexpression of the artificial PSAT1-silencing construct in Arabidopsis thaliana leads to a significant reduction of PSAT1 expression, which subsequently results in a strong inhibition of growth. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
PSAT1-silenced lines (ts-psat1.1 and ts-psat1.2) are generated for functional characterization using a microRNA-based approach. The expression of the PSAT2 gene is unaltered in PSAT1-silenced plants, phenotype, overview
additional information
deletion of the 45 N-terminal residues in mutant EhPSAT_DELTA45 results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein, with the two monomers translated and rotated by almost 180° with respect to each other, causing a rearrangement of the active site to which cofactor PLP is unable to bind. Deletions of first N-terminal 15 (EhPSAT_DELTA15) and four 11th to 14th residues (EhPSAT_DELTA4) yield up to 98% and 90% decrease in activity, respectively. Absence of aldimine linkage between PLP-Lys in the crystal structure of EhPSAT_DELTA4 mutant explains the decrease in activity and describes the importance of these N-terminal residues
additional information
-
deletion of the 45 N-terminal residues in mutant EhPSAT_DELTA45 results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein, with the two monomers translated and rotated by almost 180° with respect to each other, causing a rearrangement of the active site to which cofactor PLP is unable to bind. Deletions of first N-terminal 15 (EhPSAT_DELTA15) and four 11th to 14th residues (EhPSAT_DELTA4) yield up to 98% and 90% decrease in activity, respectively. Absence of aldimine linkage between PLP-Lys in the crystal structure of EhPSAT_DELTA4 mutant explains the decrease in activity and describes the importance of these N-terminal residues
additional information
-
deletion of the 45 N-terminal residues in mutant EhPSAT_DELTA45 results in an inactive protein, the structure shows a dimeric arrangement drastically different from that of the wild-type protein, with the two monomers translated and rotated by almost 180° with respect to each other, causing a rearrangement of the active site to which cofactor PLP is unable to bind. Deletions of first N-terminal 15 (EhPSAT_DELTA15) and four 11th to 14th residues (EhPSAT_DELTA4) yield up to 98% and 90% decrease in activity, respectively. Absence of aldimine linkage between PLP-Lys in the crystal structure of EhPSAT_DELTA4 mutant explains the decrease in activity and describes the importance of these N-terminal residues
-
additional information
phosphoserine aminotransferase (SerC) from Escherichia coli strain MG1655 is engineered to catalyze the deamination of homoserine to 4-hydroxy-2-oxobutyrate, a key reaction in producing 1,3-propanediol (1,3-PDO) from glucose in a distinct glycerol-independent metabolic pathway. An computation-based rational approach is used to change the substrate specificity of SerC from L-phosphoserine to L-homoserine, molecular dynamics simulations and virtual screening are combined to predict mutation sites. The coexpression of best mutant SerCR42W/R77W with Escherichia coli pyruvate decarboxylase and alcohol dehydrogenase results in production of 3.03 g/l of 1,3-PDO in fed-batch fermentation, which is 13fold higher than in the wild-type strain. Method evaluation, overview
additional information
-
phosphoserine aminotransferase (SerC) from Escherichia coli strain MG1655 is engineered to catalyze the deamination of homoserine to 4-hydroxy-2-oxobutyrate, a key reaction in producing 1,3-propanediol (1,3-PDO) from glucose in a distinct glycerol-independent metabolic pathway. An computation-based rational approach is used to change the substrate specificity of SerC from L-phosphoserine to L-homoserine, molecular dynamics simulations and virtual screening are combined to predict mutation sites. The coexpression of best mutant SerCR42W/R77W with Escherichia coli pyruvate decarboxylase and alcohol dehydrogenase results in production of 3.03 g/l of 1,3-PDO in fed-batch fermentation, which is 13fold higher than in the wild-type strain. Method evaluation, overview
additional information
-
phosphoserine aminotransferase (SerC) from Escherichia coli strain MG1655 is engineered to catalyze the deamination of homoserine to 4-hydroxy-2-oxobutyrate, a key reaction in producing 1,3-propanediol (1,3-PDO) from glucose in a distinct glycerol-independent metabolic pathway. An computation-based rational approach is used to change the substrate specificity of SerC from L-phosphoserine to L-homoserine, molecular dynamics simulations and virtual screening are combined to predict mutation sites. The coexpression of best mutant SerCR42W/R77W with Escherichia coli pyruvate decarboxylase and alcohol dehydrogenase results in production of 3.03 g/l of 1,3-PDO in fed-batch fermentation, which is 13fold higher than in the wild-type strain. Method evaluation, overview
-
additional information
mutant C2-A'
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Hirsch, H.; Greenberg, D.M.
Studies on phosphoserine aminotransferase of sheep brain
J. Biol. Chem.
242
2283-2287
1967
Ovis aries
brenda
Hirsch-Kolb, H.; Greenberg, D.M.
Phosphoserine aminotransferase (sheep brain)
Methods Enzymol.
17B
331-334
1971
Ovis aries
-
brenda
Lund, K.; Merrill, D.K.; Guynn, R.W.
Purification and properties of phosphoserine aminotransferase from bovine liver
Arch. Biochem. Biophys.
254
319-328
1987
Bos taurus
brenda
Basurko, M.J.; Marche, M.; Darriet, M.; Cassaigne, A.
Catalytic properties and specificity of phosphoserine aminotransferase from beef liver
Biochem. Soc. Trans.
17
787-788
1989
Bos taurus
-
brenda
Stolz, M.; Doernemann, D.
Purification, charcterization and N-terminal sequence of phosphoserine aminotransferase from the green alga Scenedesmus obliquus, mutant C-2 A'
Z. Naturforsch. C
49c
63-69
1993
Tetradesmus obliquus
-
brenda
Tanaka, T.; Yamamoto, S.; Moriya, T.; Taniguchi, M.; Hayashi, H.; Kagamiyama, H.; Oi, S.
Aspartate aminotransferase from a thermophilic formate-utilizing methanogen, Methanobacterium thermoformicicum strain SF-4: relation to serine and phosphoserine aminotransferases, but not to the aspartate aminotransferase family
J. Biochem.
115
309-317
1994
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus SF-4
brenda
Stolz, M.; Doernemann, D.
Kinetic characteristics, substrate specificity and catalytic properties of phosphoserine aminotransferase from the green alga Scenedesmus obliquus, mutant C-2A'
Z. Naturforsch. C
50c
630-637
1995
Tetradesmus obliquus
-
brenda
Battchikova, N.; Himanen, J.P.; Ahjolahti, M.; Korpela, T.
Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing
Biochim. Biophys. Acta
1295
187-194
1996
Niallia circulans
brenda
Saito, K.; Takagi, Y.; Ling, H.C.; Takahashi, H.; Noji, M.
Molecular cloning, characterization and expression of cDNA encoding phosphoserine aminotransferase involved in phosphorylated pathway of serine biosynthesis from spinach
Plant Mol. Biol.
33
359-366
1997
Spinacia oleracea
brenda
Ho, C.L.; Noji, M.; Saito, M.; Yamazaki, M.; Saito, K.
Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis from Arabidopsis
Plant J.
16
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1998
Spinacia oleracea, Arabidopsis thaliana (Q96255), Arabidopsis thaliana
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Phosphoserine aminotransferase, the second step-catalyzing enzyme for serine biosynthesis
IUBMB Life
48
525-529
1999
Bos taurus
brenda
Hester, G.; Stark, W.; Moser, M.; Kallen, J.; Markovic-Housley, Z.; Jansonius, J.N.
Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate
J. Mol. Biol.
286
829-850
1999
Escherichia coli
brenda
Baek, J.Y.; Jun do, Y.; Taub, D.; Kim, Y.H.
Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis
Biochem. J.
373
191-200
2003
Homo sapiens (Q9Y617), Homo sapiens
brenda
Peters-Wendisch, P.; Stolz, M.; Etterich, H.; Kennerknecht, N.; Sahm, H.; Eggeling, L.
Metabolic engineering of Corynebacterium glutamicum for L-serine production
Appl. Environ. Microbiol.
71
7139-7144
2005
Corynebacterium glutamicum
brenda
Dubnovitsky, A.P.; Ravelli, R.B.; Popov, A.N.; Papageorgiou, A.C.
Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage
Protein Sci.
14
1498-1507
2005
Alkalihalobacillus alcalophilus
brenda
Dubnovitsky, A.P.; Kapetaniou, E.G.; Papageorgiou, A.C.
Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus
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2005
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Arabidopsis thaliana, Entamoeba histolytica (Q60I38), Entamoeba histolytica
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Niallia circulans (Q59196), Niallia circulans
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Homo sapiens (Q9Y617), Homo sapiens
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Entamoeba histolytica
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Alkalihalobacillus alcalophilus (Q9RME2), Alkalihalobacillus alcalophilus
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Structural investigation and inhibitory response of halide on phosphoserine aminotransferase from Trichomonas vaginalis
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Trichomonas vaginalis
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Homo sapiens
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Hepatic phosphoserine aminotransferase 1 regulates insulin sensitivity in mice via Tribbles Homolog 3
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Homo sapiens
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Identification of the light-independent phosphoserine pathway as an additional source of serine in the cyanobacterium Synechocystis sp. PCC 6803
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Bombyx mori (H9JSH4), Bombyx mori (Q2F5M8), Bombyx mori, Bombyx mori p50T (H9JSH4), Bombyx mori b94 (Q2F5M8)
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Zhang, Y.; Ma, C.; Dischert, W.; Soucaille, P.; Zeng, A.P.
Engineering of phosphoserine aminotransferase increases the conversion of L-homoserine to 4-hydroxy-2-ketobutyrate in a glycerol-independent pathway of 1,3-propanediol production from glucose
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Escherichia coli (P23721), Escherichia coli, Escherichia coli MG1655 (P23721)
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Homo sapiens (Q9Y617), Homo sapiens
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Arabidopsis thaliana (Q96255), Arabidopsis thaliana (Q9SHP0)
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Structural analysis of phosphoserine aminotransferase (isoform 1) from Arabidopsis thaliana - the enzyme involved in the phosphorylated pathway of serine biosynthesis
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Arabidopsis thaliana (Q96255), Arabidopsis thaliana
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Singh, R.K.; Tomar, P.; Dharavath, S.; Kumar, S.; Gourinath, S.
N-terminal residues are crucial for quaternary structure and active site conformation for the phosphoserine aminotransferase from enteric human parasite E. histolytica
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Entamoeba histolytica (Q60I38), Entamoeba histolytica, Entamoeba histolytica HM1:IMSS (Q60I38)
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De Marchi, T.; Timmermans, M.A.; Sieuwerts, A.M.; Smid, M.; Look, M.P.; Grebenchtchikov, N.; Sweep, F.C.G.J.; Smits, J.G.; Magdolen, V.; van Deurzen, C.H.M.; Foekens, J.A.; Umar, A.; Martens, J.W.
Phosphoserine aminotransferase 1 is associated to poor outcome on tamoxifen therapy in recurrent breast cancer
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2099
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Homo sapiens (Q9Y617), Homo sapiens
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