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Information on EC 1.1.1.95 - phosphoglycerate dehydrogenase and Organism(s) Mus musculus and UniProt Accession Q61753
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1.1.1.95 phosphoglycerate dehydrogenaseIUBMB Comments
This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase .
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Word Map
- 1.1.1.95
- l-serine
- aminotransferase
- microcephaly
-
psychomotor
- hydroxymethyltransferase
-
one-carbon
- hydroxypyruvate
- l-ser
-
2-hydroxyacid
- biotechnology
- molecular biology
- synthesis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phgdh, phosphoglycerate dehydrogenase, 3-phosphoglycerate dehydrogenase, d-3-phosphoglycerate dehydrogenase, 3-pgdh, 3pgdh, pgdh3, pgdh1, ehpgdh, d-phosphoglycerate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-PGDH
-
-
-
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3-phosphoglycerate dehydrogenase
3-phosphoglyceric acid dehydrogenase
-
-
-
-
A10
-
-
-
-
alpha-phosphoglycerate dehydrogenase
-
-
-
-
D-3-phosphoglycerate dehydrogenase
D-3-phosphoglycerate:NAD oxidoreductase
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-
-
-
dehydrogenase, phosphoglycerate
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-
-
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glycerate 3-phosphate dehydrogenase
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-
-
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glycerate-1,3-phosphate dehydrogenase
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-
-
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PGDH
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-
-
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phosphoglycerate oxidoreductase
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-
-
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phosphoglyceric acid dehydrogenase
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-
-
-
3-phosphoglycerate dehydrogenase
-
-
-
-
D-3-phosphoglycerate dehydrogenase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
3-phospho-D-glycerate:NAD+ 2-oxidoreductase
This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase [6].
CAS REGISTRY NUMBER
COMMENTARY
9075-29-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
enzyme is involved in de novo L-serine biosynthesis, in the peripheral nervous system and non-neuronal tissues of mice
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
enzyme is involved in de novo L-serine biosynthesis, in the peripheral nervous system and non-neuronal tissues of mice
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
very high expression of Phgdh. It is shown that Phgdh is distributed highly in the renal papilla and inner layer of the outer zone and moderately in the cortex, whereas it is almost negative in the outer layer of the outer zone. This heterogeneous distribution is due to selective expression in distinct tubular segments, i.e., the Bowman's capsule, proximal tubule, and thin limbs of the Henle's loop
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satellite cell of the dorsal root ganglia and intestinal nerve plexuses
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located in the rostral migratory stream, high enzyme expression level
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satellite cell of the dorsal root ganglia and intestinal nerve plexuses
additional information
-
tissue expression analysis, no expression in absent in committed neuronal precursors, type A cells, derived from type C cells
-
enzyme expression in the subventricular neural progenitor cells, but not in differentiated neurons. The subventricular neural progenitor cells also show a decline in Phgdh expression in type B and C cells in the aged brain
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is required for the de novo biosynthesis of L-serine
malfunction
metabolism
physiological function
malfunction
-
Phgdh null mice have markedly decreased free serine content in their tissues, which is associated with overall growth retardation, striking brain malformation, and embryonic lethality
malfunction
-
targeted disruption of Phgdh in mice causes overall growth retardation with severe brain microcephaly and leads to embryonic lethality
malfunction
-
enzyme-depleted astrocytes accumulate 20fold less L-serine compared with controls
metabolism
-
3-phosphoglycerate dehydrogenase catalyzes the first step of the phosphorylated pathway in the de novo synthesis of L-serine. Availability of L-serine within neural stem/progenitor cells may be a critical factor for neurogenesis in developing and adult brain
metabolism
-
the enzyme catalyzes the first committed step of L-serine biosynthesis
physiological function
-
Phgdh knockout mouse embryos demonstrate that free serine and glycine concentrations are decreased markedly in head samples
physiological function
-
Phgdh null mice have markedly decreased free serine content in their tissues, which is associated with overall growth retardation, striking brain malformation, and embryonic lethality
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SERA_MOUSE
533
0
56586
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
up
-
Phgdh is transiently upregulated in the brain by kainic acid-treatment, causing selective lesions in the hippocampal region, kainic acid is injected into the bregma, overview
additional information
-
generation of Phgdh heterozygous mice, Phgdh+/-, using E14 embryonic stem cells 129P2/OlaHsd background
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PHGDH, quantitative expression analysis in wild-type and mutant mice, genotyping, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Phgdh knockout mouse embryos demonstrate that free serine and glycine concentrations are decreased markedly in head samples
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Konno, A.; Oota, Y.; Hashimoto, Y.; Kon, Y.; Iwanaga, T.
Localization of 3-phosphoglycerate dehydrogenase, an enzyme involved in de novo L-serine biosynthesis, in the peripheral nervous system and non-neuronal tissues of mice
Biomed. Res.
25
195-200
2004
Mus musculus
-
Takasaki, C.; Miura, E.; Watanabe, M.
Segmental and complementary expression of L-serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase and neutral amino acid transporter ASCT1 in the mouse kidney
Biomed. Res.
28
61-69
2007
Mus musculus (Q61753), Mus musculus
Furuya, S.; Yoshida, K.; Kawakami, Y.; Yang, J.H.; Sayano, T.; Azuma, N.; Tanaka, H.; Kuhara, S.; Hirabayashi, Y.
Inactivation of the 3-phosphoglycerate dehydrogenase gene in mice: changes in gene expression and associated regulatory networks resulting from serine deficiency
Funct. Integr. Genomics
8
235-249
2008
Homo sapiens, Mus musculus
Jeon, G.S.; Choi, D.H.; Lee, H.N.; Kim, D.W.; Chung, C.K.; Cho, S.S.
Expression of L-serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase (Phgdh) and neutral amino acid transporter ASCT1 following an excitotoxic lesion in the mouse hippocampus
Neurochem. Res.
34
827-834
2009
Mus musculus
Kinoshita, M.O.; Shinoda, Y.; Sakai, K.; Hashikawa, T.; Watanabe, M.; Machida, T.; Hirabayashi, Y.; Furuya, S.
Selective upregulation of 3-phosphoglycerate dehydrogenase (Phgdh) expression in adult subventricular zone neurogenic niche
Neurosci. Lett.
453
21-26
2009
Mus musculus
Du, H.; Vitiello, D.; Sarno, J.; Taylor, H.
3-Phosphoglycerate dehydrogenase (3-PGDH) expression is regulated by HOXA10 in murine endometrium and human endometrial cells
Reproduction
139
237-245
2009
Homo sapiens (O43175), Homo sapiens, Mus musculus (Q61753), Mus musculus
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