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PubMed2004

Mammalian target of rapamycin regulates IRS-1 serine 307 phosphorylation.

Insulin signaling can be negatively regulated by phosphorylation of serine 307 of the insulin receptor substrate (IRS)-1. Rapamycin, an inhibitor of the kinase mTOR, can prevent serine 307 phosphorylation and the development of insulin resistance. We further investigated the role of mTOR in regulating serine 307 phosphorylation, demonstrating that serine 307 phosphorylation in response to insulin, anisomycin, or tumor necrosis factor was quantitatively and temporally associated with activation of mTOR and could be inhibited by rapamycin. Amino acid stimulation activated mTOR and resulted in IRS-1 serine 307 phosphorylation without activating PKB or JNK. Okadaic acid, an inhibitor of the phosphatase PP2A, activated mTOR and stimulated the phosphorylation of serine 307 in a rapamycin-sensitive manner, indicating serine 307 phosphorylation requires mTOR activity but not PP2A, suggesting that mTOR itself may be responsible for phosphorylating serine 307. Finally, we demonstrated that serine 307 phosphorylated IRS-1 is detected primarily in the cytosolic fraction.

Adipocytes↗

PubMed2006

Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana.

A cDNA encoding a homolog of mammalian serine racemase, a unique enzyme in eukaryotes, was isolated from Arabidopsis thaliana and expressed in Escherichia coli cells. The gene product, of which the amino acid residues for binding pyridoxal 5'-phosphate (PLP) are conserved in this as well as mammalian serine racemases, catalyzes not only serine racemization but also dehydration of serine to pyruvate. The enzyme is a homodimer and requires PLP and divalent cations, Ca2+, Mg2+, Mn2+, Fe2+, or Ni2+, at alkaline pH for both activities. The racemization process is highly specific toward L-serine, whereas L-alanine, L-arginine, and L-glutamine were poor substrates. The Vmax/Km values for racemase activity of L- and D-serine are 2.0 and 1.4 nmol/mg/min/mM, respectively, and those values for L- and D-serine on dehydratase activity are 13 and 5.3 nmol/mg/min/mM, i.e. consistent with the theory of racemization reaction and the specificity of dehydration toward L-serine. Hybridization analysis showed that the serine racemase gene was expressed in various organs of A. thaliana.

Alanine↗

PubMed1998

Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants--structural and kinetic properties of the free and bound enzymes.

The last steps of cysteine synthesis in plants involve two consecutive enzymes. The first enzyme, serine acetyltransferase, catalyses the acetylation of L-serine in the presence of acetyl-CoA to form O-acetylserine. The second enzyme, O-acetylserine (thiol) lyase, converts O-acetylserine to L-cysteine in the presence of sulfide. We have, in the present work, over-produced in Escherichia coli harboring various type of plasmids, either a plant serine acetyltransferase or this enzyme with a plant O-acetylserine (thiol) lyase. The free recombinant serine acetyltransferase (subunit mass of 34 kDa) exhibited a high propensity to form high-molecular-mass aggregates and was found to be highly unstable in solution. However, these aggregates were prevented in the presence of O-acetylserine (thiol) lyase (subunit mass of 36 kDa). Under these conditions homotetrameric serine acetyltransferase associated with two molecules of homodimeric O-acetylserine (thiol) lyase to form a bienzyme complex (molecular mass approximately 300 kDa) called cysteine synthase containing 4 mol pyridoxal 5'-phosphate/mol complex. O-Acetylserine triggered the dissociation of the bienzyme complex, whereas sulfide counteracted the action of O-acetylserine. Protein-protein interactions within the bienzyme complex strongly modified the kinetic properties of plant serine acetyltransferase: there was a transition from a typical Michaelis-Menten model to a model displaying positive kinetic co-operativity with respect to serine and acetyl-CoA. On the other hand, the formation of the bienzyme complex resulted in a very dramatic decrease in the catalytic efficiency of bound O-acetylserine (thiol) lyase. The latter enzyme behaved as if it were a structural and/or regulatory subunit of serine acetyltransferase. Our results also indicated that bound serine acetyltransferase produces a build-up of O-acetylserine along the reaction path and that the full capacity for cysteine synthesis can only be achieved in the presence of a large excess of free O-acetylserine (thiol) lyase. These findings contradict the widely held belief that such a bienzyme complex is required to channel the metabolite intermediate O-acetylserine.

Acetyltransferases↗

PubMed1983

Control of hepatic utilization of serine, glycine and threonine in fed and starved rats.

Effects of varying protein level on hepatic utilization of serine, threonine and glycine were examined by measurements of metabolic fluxes across the liver. Feeding a high protein (HP) diet markedly enhanced hepatic extraction of serine, threonine and glycine, in parallel to alanine. After 20 hours starvation, activity of alanine aminotransferase and serine dehydratase still reflected the induction of these enzymes in fed rats. Thus, in starved rats previously adapted to HP diets, hepatic uptake of serine, threonine and glycine remained very efficient. With a normal diet, gluconeogenesis from alanine may be very active during starvation, in contrast to serine. The present results suggest that serine, and, to a lesser extent glycine, are very efficient glucogenic substrates with HP diets. The serine aminotransferase pathway might be important in rats fed HP diets, particularly for utilization of serine synthesized from glycine in mitochondria. With HP diets, the drop in hepatic alanine, serine and threonine suggest that transport across the plasma membrane might limit their utilization.

Alanine↗

PubMed2004

The N-methyl D-aspartate receptor glycine site and D-serine metabolism: an evolutionary perspective.

The N-methyl D-aspartate (NMDA) type of glutamate receptor requires two distinct agonists to operate. Glycine is assumed to be the endogenous ligand for the NMDA receptor glycine site, but this notion has been challenged by the discovery of high levels of endogenous d-serine in the mammalian forebrain. I have outlined an evolutionary framework for the appearance of a glycine site in animals and the metabolic events leading to high levels of D-serine in brain. Sequence alignments of the glycine-binding regions, along with the scant experimental data available, suggest that the properties of invertebrate NMDA receptor glycine sites are probably different from those in vertebrates. The synthesis of D-serine in brain is due to a pyridoxal-5'-phosphate (B(6))-requiring serine racemase in glia. Although it remains unknown when serine racemase first evolved, data concerning the evolution of B(6) enzymes, along with the known occurrences of serine racemases in animals, point to D-serine synthesis arising around the divergence time of arthropods. D-Serine catabolism occurs via the ancient peroxisomal enzyme d-amino acid oxidase (DAO), whose ontogenetic expression in the hindbrain of mammals is delayed until the postnatal period and absent from the forebrain. The phylogeny of D-serine metabolism has relevance to our understanding of brain ontogeny, schizophrenia and neurotransmitter dynamics.

Amino Acid Oxidoreductases↗

PubMed2002

Establishment of a simple assay in vitro for hepatitis C virus NS3 serine protease based on recombinant substrate and single-chain protease.

AIM: To establish a simple and convenient assay in vitro for the Hepatitis C virus NS3 serine protease based on the recombinant protease and substrate, and to evaluate its feasibility in screening the enzyme inhibitors. METHODS: Based on the crystallographic structure of hepatitis C virus (HCV) serine protease, a novel single-chain serine protease was designed, in which the central sequence of cofactor NS4A was linked to the N-terminus of NS3 serine protease domain via a flexible linker GSGS. The fusion gene was obtained by two-step PCR that was carried out with three primers and then cloned into the prokaryotic expression vector pQE30, and the recombinant clone was verified by DNA sequencing. The single-chain recombinant protease was expressed when the E.coli was induced with IPTG and the expression conditions were optimized to produce large amount of soluble protease. The recombinant substrate NS5ab that covers the cleavage point NS5A/B was also expressed in E.coli. Both of the protease and substrate were purified by using Ni-NTA agarose metal affinity resin, then they were mixed together in a specific buffer, and the mixture was analyzed by SDS-PAGE. The cleavage system was used to evaluate some compounds for their inhibitory activity on serine protease. RESULTS: The single-chain recombinant protease was over-expressed as soluble protein when the E.coli was induced at a low dosage of IPTG (0.2 mM) and cultured at a low temperature (15 degrees ). The protease was purified by using Ni-NTA agarose metal affinity resin (the purity is over 95 %). The recombinant substrate NS5ab was expressed in an insoluble form and could refold successfully after purification and dialysis. A simple and convenient assay in vitro was established, in which the purified single-chain serine protease could cleave the recombinant substrate NS5ab into two fragments that were visualized by SDS-PAGE. PMSF had an effect on inhibiting activity of serine protease, while EDTA had not. CONCLUSION: A simple and convenient assay in vitro for hepatitis C virus NS3 serine protease is based on recombinant substrate NS5ab and single-chain serine protease. This assay can be used in screening of enzyme inhibitors.

Amino Acid Sequence↗

PubMed2000

[Endogenous D-serine in mammalian brains].

It is well established that, like glycine and D-alanine, D-serine potentiates glutamate neurotransmission via the N-methyl-D-aspartate (NMDA) receptor by selective stimulation of its strychnine-insensitive glycine site and acts as a co-agonist of the glutamate receptor. D-Serine has been found to modify behavioral changes associated with higher brain functions such as memory, convulsion, anxiety, psychotomimetic-induced abnormal behavior and cerebellar ataxia. Interestingly, a substantial amount of free D-serine has been demonstrated in mammalian brains, although it has long been presumed that D-amino acids are uncommon in mammals. Free D-serine is predominantly concentrated in the brain with a persistent high content throughout life. The patterns of the regional variations and the postnatal changes in brain D-serine are closely correlated with those of the R2B subunit of the N-methyl-D-aspartate (NMDA) type excitatory amino acid receptor. Moreover, D-serine is released to the extracellular space and taken up into the brain homogenates, C6 glioma cells and primary culture of astrocytes of the rat cerebral cortex. Recently, the conversion of L-serine to its D-form by serine racemase has been suggested by in vivo and in vitro experiments. These data are consistent with the view that D-serine might be an intrinsic positive modulator of the brain NMDA receptor containing the R2B subunit and play a pivotal role in controlling behavioral expression in mammals.

Animals↗

PubMed1989

The role of Ca2+ and Mg2+ in the cytotoxic T lymphocyte reaction and in the secretion of N alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester-serine esterase by human T cell clones.

Human T cell clones contain enzymes that can cleave the substrate N-alpha-benzyloxycarbonyl-L-lysine thiobenzyl ester (BLT). All CTL clones tested in this study secreted BLT-serine esterase activity, whereas only one of three tested non-cytolytic T cell clones secreted this enzymatic activity upon Ag-specific activation. BLT-serine esterase secretion could also be induced by the Fc gamma+ target cell Daudi in the presence of mAb specific for the TCR/CD3 complex, CD2, or the T cell activation Ag Tp 103. In addition, anti-CD3 and a mitogenic combination of anti-CD2 mAb, induced secretion of BLT-serine esterase in the absence of target cells, whereas anti-Tp 103 failed to do so. The secreted BLT-serine esterase activity induced by the various ligands was inhibited by the serine esterase inhibitors PMSF and m-ABA, but not by N-alpha-p-tosyl-L-lysine chloromethyl ketone. Significant BLT-serine esterase activity was induced by target cells or soluble anti-CD3 in the absence of extracellular Ca2+ ions, provided that extracellular Mg2+ ions were present. The cytotoxic activities by the human CTL clones were completely blocked under these conditions. All ligands that induced BLT-serine esterase secretion in the absence of extracellular Ca2+, induced a transient rise of intracellular Ca2+. Soluble anti-CD3 mAb did not induce a transient rise in intracellular Ca2+ or secretion of BLT serine esterase in CTL preincubated for 2 h with 5 mM EGTA. These findings indicate that mobilization of intracellular Ca2+ in human CTL clones is required for induction of secretion of BLT-serine esterase.

Antibodies, Monoclonal↗

PubMed2006

D-serine in the developing human central nervous system.

To elucidate the role of D-serine in human central nervous system, we analyzed D-serine, L-serine, and glycine concentrations in cerebrospinal fluid of healthy children and children with a defective L-serine biosynthesis (3-phosphoglycerate dehydrogenase deficiency). Healthy children showed high D-serine concentrations immediately after birth, both absolutely and relative to glycine and L-serine, declining to low values at infancy. D-Serine concentrations were almost undetectable in untreated 3-phosphoglycerate dehydrogenase-deficient patients. In one patient treated prenatally, D-serine concentration was nearly normal at birth and the clinical phenotype was normal. These observations suggest a pivotal role for D-serine in normal and aberrant human brain development.

Central Nervous System↗

PubMed2004

Simultaneous determination of D- and L-serine in rat brain microdialysis sample using a column-switching HPLC with fluorimetric detection.

Both D- and L-serine in rat brain microdialysis sample were simultaneously determined by pre-column fluorescence derivatization with 4-fluoro-7-nitro-2,1,3-benzoxadiazole (NBD-F), separation of the derivatives on ODS column, TSKgel ODS-80TsQA, followed by Pirkle type chiral columns, Sumichiral OA-2500 (S), which gave a sufficient enantiomeric separation of NBD-D-serine and NBD-L-serine, and fluorimetric detection at a wavelength of 540 nm with an excitation wavelength of 470 nm. The peaks of NBD-D-serine and NBD-L-serine in the rat brain microdialysis sample were clearly found, and the validation study showed satisfactory results; the precision and accuracy were within 5.14 and 109%, respectively. Using the proposed HPLC method, the time-course profile of D-serine concentration in rat prefrontal cortex following intraperitoneal administration of D-serine was investigated. As a consequence, D-serine appeared to be rapidly distributed in the brain, and then decreased gradually with time in the extracellular fluid of the rat prefrontal cortex. The proposed HPLC method will be useful for in vivo studies on D-serine, which acts as a coagonist for N-methyl-D-aspartate receptor, to the extracellular fluid of rat brain.

4-Chloro-7-nitrobenzofurazan↗

PubMed2002

Transport of D-serine via the amino acid transporter ATB(0,+) expressed in the colon.

D-Serine, synthesized endogenously in the brain, is an important modulator of glutamatergic neurotransmission. Since colonic bacteria produce D-serine, we asked the question whether there are transport mechanisms in the colon that might make this exogenously produced D-serine available to the host. Here we identify for the first time an amino acid transporter in the intestine for high-affinity active transport of D-serine. This transporter, called ATB(0,+), is a Na(+)- and Cl(-)-coupled transporter for L-enantiomers of neutral and cationic amino acids. Here we demonstrate that ATB(0,+) is also capable of mediating the Na(+)- and Cl(-)-coupled transport of D-serine. The affinity of ATB(0,+) for L-serine and D-serine is similar, the K(t) value for the two enantiomers being approximately 150 microM. In addition to D-serine, ATB(0,+) transports D-alanine, D-methionine, D-leucine, and D-tryptophan. However, several other neutral and cationic amino acids that are transportable substrates for ATB(0,+) as L-enantiomers are not transported when presented as D-enantiomers. ATB(0,+) is expressed in the intestinal tract, interestingly not in the proximal intestine but in the distal intestine. Expression is most predominant in the colon where the transporter is localized to the luminal membrane of colonocytes, making this transporter uniquely suitable for absorption of bacteria-derived D-serine.

Amino Acid Transport Systems, Basic↗

PubMed1995

Free D-serine in post-mortem brains and spinal cords of individuals with and without neuropsychiatric diseases.

We have measured the concentrations of free D-serine post-mortem in the prefrontal cortex, parietal cortex, cerebellum and spinal cord from individuals with and without (controls) neuropsychiatric diseases using high-performance liquid chromatography with fluorometric detection. The levels of D-serine were found to be high in the prefrontal and parietal cortex (around 100 nmol/g wet weight) and very low in the cerebellum and spinal cord (below 10 nmol/g wet weight). The uneven distribution of the D-amino acid in the human central nervous system (CNS) resembles that observed in rodents, suggesting that, as shown in the rat CNS, the regional variation of D-serine content in the human brain might also be closely correlated with those of the N-methyl-D-aspartate (NMDA) type excitatory amino acid receptor. In the prefrontal cortex, the gray and white matter had a similar concentration of D-serine. These findings, together with the selective action of D-serine at the NMDA-related glycine site and the non-neurogenic nature of extracellular D-serine release, add further support to the view that D-serine could be an intrinsic modulator of the NMDA receptor liberated from certain glial cells in the mammalian brain. Despite the anti-psychotogen activity of D-serine in the rat, there were no statistically significant differences between the D-serine contents in the prefrontal or parietal cortex of controls and those of patients with schizophrenia or dementia of the Alzheimer type.

Aging↗

PubMed1991

Protection against 2-methoxyethanol-induced teratogenesis by serine enantiomers: studies of potential alteration of 2-methoxyethanol pharmacokinetics.

Several simple physiological compounds attenuate the teratogenic effects of 2-methoxyethanol (2-ME) when coadministered with 2-ME to mice. The mechanism of this protective action, however, has not been elucidated. Alteration of the kinetics of 2-ME and its oxidation product 2-methoxyacetic acid (2-MAA), the putative ultimate toxicant, was considered. D-Serine, the most efficacious attenuator, and L-serine (both 16.5 mmol/kg po) were examined for their abilities to mitigate 2-ME teratogenicity and to alter the disposition of an oral or sc bolus dose of 2-ME (3.3 mmol/kg containing 6 microCi 2-[methoxy-14C]ethanol) given to CD-1 mice on Gestation Day 11. L-Serine reduced the incidence of malformed fetuses from greater than or equal to 72% to 26-28%, while only 18 and 9% of fetuses were affected after coadministration of D-serine with sc and po 2-ME, respectively. Changes in the metabolism of orally administered 2-[14C]ME were specific to each enantiomer. D-Serine reduced the amount of 2-methoxy-N-acetylglycine eliminated in the urine to 70-75% of values observed with 2-ME alone, and concurrently increased the amount of urinary 2-MAA. L-Serine induced an initially higher rate of 14CO2 exhalation. Both enantiomers delayed gastrointestinal absorption of 2-ME, and significantly reduced 2-MAA levels in maternal plasma during the first hour after dosing. This resulted in a nonsignificant decrease (10-17%) in total embryonic exposure to 2-MAA. However, when 2-ME was injected sc, maternal plasma 2-ME/2-MAA pharmacokinetics were not affected by serine. In addition, dosing with 2.3 and 1.3 mmol 2-ME/kg sc alone showed that the embryo 2-MAA exposure levels which cause malformations in less than or equal to 35% fetuses were considerably lower than those measured following serine plus 3.3 mmol 2-ME/kg (po or sc). These data infer that serine does not protect against 2-ME-induced teratogenicity by altering 2-ME pharmacokinetics and reducing 2-MAA levels in the embryo.

Animals↗

PubMed1996

Modulation of glycine-serine interconversion by TCA and glycolytic intermediates in normoxic and hypoxic proximal tubules.

Glycine-serine interconversion is important to numerous metabolic processes and serine release by the kidney. Incubation of freshly isolated rat renal proximal tubules with 5 mM glycine 75% 13C-labelled in the 2-position resulted in 13C-labelled incorporation into serine of 69 micromol.g protein(-1) (+/- 14, n = 16) at 20 min. Addition of 5 mM glucose, 4 mM lactate, 1 mM alanine, 1 mM butyrate and 1 mM glutamate increased 13C-label incorporation into serine to 173 micromol.g protein(-1) (+/- 32, n = 4) at 60 min, 50% greater than tubules incubated with 5 mM glycine alone (P < 0.05). The increase was prevented by hypoxia. Reoxygenation for 20 min restored the rate of incorporation of 13C-label into serine. The fraction of unlabelled serine remained approximately 47% at 20, 40 and 60 min in each group. The results indicate that in the presence of oxygen, TCA and glycolytic intermediates stimulate serine synthesis via the glycine cleavage complex and serine hydroxymethyltransferase pathways and not the phosphorylated pathway. In addition, significant serine production occurs from an unidentified source, which is also tightly coupled to glycine metabolism. Both in the presence and absence of added TCA and glycolytic intermediates, glycine was the principle source of the methylene group in methylene tetrahydrofolate.

Animals↗

PubMed1993

Serine released from hippocampal slices during deprivation of oxygen and glucose enhances the effects of glutamate on neuronal function.

Using guinea-pig hippocampal slices, we determined the amount of various amino acids released into the medium during deprivation of oxygen and glucose. Within 10 min of slices being deprived of O2 and glucose, the amounts of serine, aspartate, alanine, glycine, GABA, taurine and threonine released into the medium increased up to 1.7 (serine), 1.6 (aspartate), 1.6 (alanine), 1.9 (glycine), 2.0 (GABA), 1.4 (taurine) and 1.8 (threonine) times the control levels, respectively. The amount of serine released 10 min after O2 and glucose deprivation was four times as great as that of glutamate. The dose-response effects of glutamate and serine were studied on the population spikes evoked in the granular cell layer. Bath application of 100 microM serine elevated the amplitude of the population spike to 117% and at 10 mM depressed it completely. The dose-response curve for glutamate displayed a similar pattern but the effectiveness was 10 times higher than that of serine. The combined application of glutamate (300 microM) and serine (2 mM) produced a dramatic reduction in and depression of the amplitude of the population spike, although 300 microM glutamate and 2 mM serine individually failed to show a significant effect. The population spike was depressed by the addition of 1 mM glutamate but, after washing, it recovered completely. On the other hand treatment with 1 mM glutamate together with 5 mM serine caused no recovery of the population spike even after removal of the agents.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Triphosphate↗

PubMed2004

Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae.

The pH dependence of kinetic parameters was determined in both reaction directions to obtain information about the acid-base chemical mechanism of serine acetyltransferase from Haemophilus influenzae (HiSAT). The maximum rates in both reaction directions, as well as the V/K(serine) and V/K(OAS), decrease at low pH, exhibiting a pK of approximately 7 for a single enzyme residue that must be unprotonated for optimum activity. The pH-independent values of V(1)/E(t), V(1)/K(serine)E(t), V/K(AcCoA)E(t), V(2)/E(t), V(2)/K(OAS)E(t), and V/K(CoA)E(t) are 3300 +/- 180 s(-1), (9.6 +/- 0.4) x 10(5) M(-1) s(-1), 3.3 x 10(6) M(-1) s(-1), 420 +/- 50 s(-1), (2.1 +/- 0.5) x 10(4) M(-1) s(-1), and (4.2 +/- 0.7) x 10(5) M(-1) s(-1), respectively. The K(i) values for the competitive inhibitors glycine and l-cysteine are pH-independent. The solvent deuterium kinetic isotope effects on V and V/K in the direction of serine acetylation are 1.9 +/- 0.2 and 2.5 +/- 0.4, respectively, and the proton inventories are linear for both parameters. Data are consistent with a single proton in flight in the rate-limiting transition state. A general base catalytic mechanism is proposed for the serine acetyltransferase. Once acetyl-CoA and l-serine are bound, an enzymic general base accepts a proton from the l-serine side chain hydroxyl as it undergoes a nucleophilic attack on the carbonyl of acetyl-CoA. The same enzyme residue then functions as a general acid, donating a proton to the sulfur atom of CoASH as the tetrahedral intermediate collapses, generating the products OAS and CoASH. The rate-limiting step in the reaction at limiting l-serine levels is likely formation of the tetrahedral intermediate between serine and acetyl-CoA.

Acetylation↗

PubMed2005

Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28.

The Ras-mitogen activated protein kinase (Ras-MAPK) pathway plays an integral role in the formation of human malignancies. Stimulation of this pathway results in phosphorylation of histone H3 at serines 10 and 28 and expression of immediate-early genes. Phosphorylated (serine 10) H3, which is also acetylated on lysine 14, is associated with immediate-early genes. In this report, we investigated the relationship between these two H3 phosphorylation events in parental and ras-transformed fibroblasts. Immunoblot analyses of two-dimensional gel patterns demonstrated that all three H3 variants were phosphorylated after stimulation of the Ras-MAPK pathway and during mitosis. Following stimulation of the Ras-MAPK pathway, H3 phosphorylated on serines 10 and 28 was excluded from regions of highly condensed chromatin and was present in increased levels in ras-transformed cells. Although H3 phosphorylated at serine 10 or 28 was dynamically acetylated, H3 phosphorylated at serine 28 had a higher steady state of acetylation than that of H3 phosphorylated at serine 10. When visualized with indirect immunofluorescence, most foci of phosphorylated serine 28 H3 did not co-localize with foci of H3 phosphorylated on serine 10 or phosphoacetylated on serine 10 and lysine 14, suggesting that these two phosphorylation events act separately to promote gene expression.

Animals↗

PubMed1971

Aspects of glycine and serine biosynthesis during growth of Pseudomonas AM1 on C compounds.

1. Methanol or formate can replace serine or glycine as supplements for growth on succinate of the auxotrophic mutants 20S and 82G of Pseudomonas AM1, showing that the organism can synthesize glycine and serine in net fashion from C(1) units. 2. Double mutants of Pseudomonas 20S and 82G have been prepared (20ST-1 and 82GT-1) that are unable to grow on succinate+1mm-glyoxylate, succinate+2mm-methanol or methanol alone. 3. Mutants 20ST-1 and 82GT-1 lacked serine-glyoxylate aminotransferase activity, and revertants to the phenotype of 20S and 82G regained serine-glyoxylate aminotransferase activity. A total revertant of 82GT-1 to wild-type phenotype regained activities of serine hydroxymethyltransferase and serine-glyoxylate aminotransferase. 4. The activity of serine-glyoxylate aminotransferase in methanol-grown Pseudomonas AM1 is eightfold higher than in the succinate-grown organism. 5. The combined results show that in Pseudomonas AM1 serine-glyoxylate aminotransferase is necessary for growth on C(1) compounds and is involved in the conversion of methanol into glycine via glyoxylate. 6. It is suggested that the phosphorylated pathway of serine biosynthesis from phosphoglycerate replenishes the supply of alpha-amino groups necessary for the flow of glyoxylate through the main assimilatory pathway during growth on C(1) compounds.

Carbon↗