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Article ; Online: Deficiency in L-serine deaminase interferes with one-carbon metabolism and cell wall synthesis in Escherichia coli K-12.

Zhang, Xiao / El-Hajj, Ziad W / Newman, Elaine

2010 Volume 192, Issue 20, Page(s) 5515–5525

Abstract: Escherichia coli K-12 provided with glucose and a mixture of amino acids depletes L-serine more ... serine deaminases (SdaA, SdaB, and TdcG) of E. coli K-12 is unable to do this. The high level of L-serine ... quickly than any other amino acid even in the presence of ammonium sulfate. A mutant without three 4Fe4S L ...

Abstract	Escherichia coli K-12 provided with glucose and a mixture of amino acids depletes L-serine more quickly than any other amino acid even in the presence of ammonium sulfate. A mutant without three 4Fe4S L-serine deaminases (SdaA, SdaB, and TdcG) of E. coli K-12 is unable to do this. The high level of L-serine that accumulates when such a mutant is exposed to amino acid mixtures starves the cells for C(1) units and interferes with cell wall synthesis. We suggest that at high concentrations, L-serine decreases synthesis of UDP-N-acetylmuramate-L-alanine by the murC-encoded ligase, weakening the cell wall and producing misshapen cells and lysis. The inhibition by high L-serine is overcome in several ways: by a large concentration of L-alanine, by overproducing MurC together with a low concentration of L-alanine, and by overproducing FtsW, thus promoting septal assembly and also by overexpression of the glycine cleavage operon. S-Adenosylmethionine reduces lysis and allows an extensive increase in biomass without improving cell division. This suggests that E. coli has a metabolic trigger for cell division. Without that reaction, if no other inhibition occurs, other metabolic functions can continue and cells can elongate and replicate their DNA, reaching at least 180 times their usual length, but cannot divide.
MeSH term(s)	Alanine/metabolism ; Amino Acids/chemistry ; Amino Acids/metabolism ; Carbon/metabolism ; Cell Wall/metabolism ; Culture Media/chemistry ; Escherichia coli K12/genetics ; Escherichia coli K12/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Expression Regulation, Bacterial/physiology ; Glucose/chemistry ; Glucose/metabolism ; Hypoxanthine/metabolism ; L-Serine Dehydratase/deficiency ; Mutation ; Promoter Regions, Genetic ; Serine/metabolism
Chemical Substances	Amino Acids ; Culture Media ; Escherichia coli Proteins ; casamino acids ; Hypoxanthine (2TN51YD919) ; Serine (452VLY9402) ; Carbon (7440-44-0) ; L-Serine Dehydratase (EC 4.3.1.17) ; Glucose (IY9XDZ35W2) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2010-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.00748-10
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Article ; Online: Deficiency in l-serine deaminase results in abnormal growth and cell division of Escherichia coli K-12.

Zhang, Xiao / Newman, Elaine

Molecular microbiology

2008 Volume 69, Issue 4, Page(s) 870–881

Abstract: ... in Escherichia coli K-12. A strain from which the three genes (sdaA, sdaB, tdcG) coding for this organism's three l ... The loss of the ability to deaminate l-serine severely impairs growth and cell division ... by methylation, that an unusually high intracellular l-serine concentration, in the presence of other amino acids ...

Abstract	The loss of the ability to deaminate l-serine severely impairs growth and cell division in Escherichia coli K-12. A strain from which the three genes (sdaA, sdaB, tdcG) coding for this organism's three l-serine deaminases had been deleted grows well in glucose minimal medium but, on subculture into minimal medium with glucose and casamino acids, it makes very large, abnormally shaped cells, many of which lyse. When inoculated into Luria-Bertani (LB) broth with or without glucose, it makes very long filaments. Provision of S-adenosylmethionine restores cell division in LB broth with glucose, and repairs much of the difficulty in growth in medium with casamino acids. We suggest that replication of E. coli is regulated by methylation, that an unusually high intracellular l-serine concentration, in the presence of other amino acids, starves the cell for S-adenosylmethionine and that it is the absence of S-adenosylmethionine and/or of C1-tetrahydrofolate derivatives that prevents normal cell division.
MeSH term(s)	Amino Acids/metabolism ; Amino Acids/pharmacology ; Cell Division/genetics ; Culture Media/metabolism ; Culture Media/pharmacology ; Escherichia coli/cytology ; Escherichia coli/drug effects ; Escherichia coli/enzymology ; Escherichia coli/growth & development ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Deletion ; L-Serine Dehydratase/genetics ; L-Serine Dehydratase/metabolism ; S-Adenosylmethionine/metabolism ; S-Adenosylmethionine/pharmacology
Chemical Substances	Amino Acids ; Culture Media ; Escherichia coli Proteins ; casamino acids ; S-Adenosylmethionine (7LP2MPO46S) ; L-Serine Dehydratase (EC 4.3.1.17)
Language	English
Publishing date	2008-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/j.1365-2958.2008.06315.x
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Article: Deficiency in l-serine deaminase results in abnormal growth and cell division of Escherichia coli K-12

Zhang, Xiao / Newman, Elaine

Molecular microbiology. 2008 Aug., v. 69, no. 4

2008

Abstract	The loss of the ability to deaminate l-serine severely impairs growth and cell division in Escherichia coli K-12. A strain from which the three genes (sdaA, sdaB, tdcG) coding for this organism's three l-serine deaminases had been deleted grows well in glucose minimal medium but, on subculture into minimal medium with glucose and casamino acids, it makes very large, abnormally shaped cells, many of which lyse. When inoculated into Luria-Bertani (LB) broth with or without glucose, it makes very long filaments. Provision of S-adenosylmethionine restores cell division in LB broth with glucose, and repairs much of the difficulty in growth in medium with casamino acids. We suggest that replication of E. coli is regulated by methylation, that an unusually high intracellular l-serine concentration, in the presence of other amino acids, starves the cell for S-adenosylmethionine and that it is the absence of S-adenosylmethionine and/or of C1-tetrahydrofolate derivatives that prevents normal cell division.
Language	English
Dates of publication	2008-08
Size	p. 870-881.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/j.1365-2958.2008.06315.x
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Article: A novel L-serine deaminase activity in Escherichia coli K-12.

Su, H / Newman, E B

Journal of bacteriology

1991 Volume 173, Issue 8, Page(s) 2473–2480

Abstract: We demonstrate here that Escherichia coli K-12 synthesizes two different L-serine deaminases (L-SD ... catalyzing the nonoxidative deamination of L-serine to pyruvate, one coded for by the previously described ... sdaA gene and a second, hitherto undescribed enzyme which we call L-SD2. A strain carrying a null ...

Abstract	We demonstrate here that Escherichia coli K-12 synthesizes two different L-serine deaminases (L-SD) catalyzing the nonoxidative deamination of L-serine to pyruvate, one coded for by the previously described sdaA gene and a second, hitherto undescribed enzyme which we call L-SD2. A strain carrying a null mutation in sdaA made no detectable L-SD in minimal medium, but had activity in Luria broth. We describe a mutation, sdaX, which affects the regulation of L-SD2 and permits its expression in minimal medium, and an insertion mutation, sdaB, which abolishes L-SD2 activity completely. Both mutations lie near 60.5 min on the E. coli genetic map. The two L-SD enzymes have similar enzyme parameters, and both require posttranslational activation.
MeSH term(s)	Chromosome Mapping ; Cloning, Molecular ; Conjugation, Genetic ; Dithiothreitol/pharmacology ; Escherichia coli/metabolism ; Iron/pharmacology ; L-Serine Dehydratase/biosynthesis ; L-Serine Dehydratase/genetics ; Nucleic Acid Hybridization ; Plasmids ; Transduction, Genetic
Chemical Substances	Iron (E1UOL152H7) ; L-Serine Dehydratase (EC 4.3.1.17) ; Dithiothreitol (T8ID5YZU6Y)
Language	English
Publishing date	1991-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/jb.173.8.2473-2480.1991
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Article: An estimate of the extent of deamination of L-serine in auxotrophs of Escherichia coli K-12.

Ramotar, D / Newman, E B

Canadian journal of microbiology

1986 Volume 32, Issue 11, Page(s) 842–846

Abstract: We have shown that serine-glycine auxotrophs of Escherichia coli K-12 use exogenous L-serine ... inefficiently as a source of biosynthetic intermediates. Much of the L-serine supplied in the medium is not used ... to satisfy the auxotrophic requirement, owing to its diversion by L-serine deaminase, presumably to pyruvate ...

Abstract	We have shown that serine-glycine auxotrophs of Escherichia coli K-12 use exogenous L-serine inefficiently as a source of biosynthetic intermediates. Much of the L-serine supplied in the medium is not used to satisfy the auxotrophic requirement, owing to its diversion by L-serine deaminase, presumably to pyruvate. This is the first proof that the activity known as L-serine deaminase actually deaminates L-serine in vivo.
MeSH term(s)	Culture Media ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli/growth & development ; Glycine/metabolism ; L-Serine Dehydratase/metabolism ; Mutation ; Serine/metabolism
Chemical Substances	Culture Media ; Serine (452VLY9402) ; L-Serine Dehydratase (EC 4.3.1.17) ; Glycine (TE7660XO1C)
Language	English
Publishing date	1986-11
Publishing country	Canada
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	280534-0
ISSN	1480-3275 ; 0008-4166
ISSN (online)	1480-3275
ISSN	0008-4166
DOI	10.1139/m86-155
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Article: Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12.

Su, H / Moniakis, J / Newman, E B

European journal of biochemistry

1993 Volume 211, Issue 3, Page(s) 521–527

Abstract: ... gene fusions results in the copurification of L-serine deaminase 1. We conclude that sdaA is the structural ... gene for the latter enzyme. The purified L-serine deaminase 1 obtained after collagenase treatment ...

Abstract	The purification by affinity chromatography of beta-galactosidase from strains carrying sdaA/lacZ gene fusions results in the copurification of L-serine deaminase 1. We conclude that sdaA is the structural gene for the latter enzyme. The purified L-serine deaminase 1 obtained after collagenase treatment of an sdaA-collagen-lacZ fusion differs from the native enzyme by the addition of several amino acids at the C-terminal. Like the enzyme in crude extracts, this purified enzyme is catalytically inactive, and is activated by incubation with iron and dithiothreitol.
MeSH term(s)	Base Sequence ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; Collagen/genetics ; Collagenases/metabolism ; Dithiothreitol/pharmacology ; Enzyme Activation/drug effects ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Genes, Bacterial ; Iron/pharmacology ; L-Serine Dehydratase/genetics ; L-Serine Dehydratase/isolation & purification ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Plasmids ; Recombinant Fusion Proteins/isolation & purification ; Recombinant Fusion Proteins/metabolism ; beta-Galactosidase/genetics ; beta-Galactosidase/isolation & purification
Chemical Substances	Recombinant Fusion Proteins ; Collagen (9007-34-5) ; Iron (E1UOL152H7) ; beta-Galactosidase (EC 3.2.1.23) ; Collagenases (EC 3.4.24.-) ; L-Serine Dehydratase (EC 4.3.1.17) ; Dithiothreitol (T8ID5YZU6Y)
Language	English
Publishing date	1993-02-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1111/j.1432-1033.1993.tb17578.x
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Article: The leucine regulon of Escherichia coli K-12: a mutation in rblA alters expression of L-leucine-dependent metabolic operons.

Tuan, L R / D'Ari, R / Newman, E B

Journal of bacteriology

1990 Volume 172, Issue 8, Page(s) 4529–4535

Abstract: ... by leucine. Selected for its ability to grow with L-serine as sole carbon source, the rbl-1::Tn10 mutant had ... high levels of L-serine deaminase activity (due to increased transcription of the structural gene) and ... of another amino acid-degrading enzyme, L-threonine dehydrogenase, and decreased transcription of the operons serA and ...

Abstract	We have isolated and characterized a highly pleiotropic Escherichia coli mutant affected in the activity of a number of enzymes involved in different metabolic pathways, all of which are regulated by leucine. Selected for its ability to grow with L-serine as sole carbon source, the rbl-1::Tn10 mutant had high levels of L-serine deaminase activity (due to increased transcription of the structural gene) and of another amino acid-degrading enzyme, L-threonine dehydrogenase, and decreased transcription of the operons serA and ilvIH, coding for biosynthetic enzymes. The rbl mutation suppressed the slow growth of a metK mutant, deficient in S-adenosylmethionine synthetase. Furthermore, metK mutants spontaneously accumulated faster-growing rbl-like derivatives, and a commonly used metK strain, RG62, carries such a mutation. The rbl gene is located near 20 min on the E. coli genetic map. All phenotypes of the rbl mutant could be observed in rbl+ strains cultivated in the presence of L-leucine, and exogenous L-leucine had little further effect on the rbl strains. We propose that the rbl gene product is the regulator of a global response to leucine.
MeSH term(s)	Alcohol Oxidoreductases/genetics ; Alcohol Oxidoreductases/metabolism ; DNA Transposable Elements ; Escherichia coli/genetics ; Genes, Regulator ; Genotype ; L-Serine Dehydratase/genetics ; L-Serine Dehydratase/metabolism ; Leucine/metabolism ; Methionine Adenosyltransferase/genetics ; Mutation ; Operon ; Transcription, Genetic ; beta-Galactosidase/genetics ; beta-Galactosidase/metabolism
Chemical Substances	DNA Transposable Elements ; Alcohol Oxidoreductases (EC 1.1.-) ; L-threonine 3-dehydrogenase (EC 1.1.1.103) ; Methionine Adenosyltransferase (EC 2.5.1.6) ; beta-Galactosidase (EC 3.2.1.23) ; L-Serine Dehydratase (EC 4.3.1.17) ; Leucine (GMW67QNF9C)
Language	English
Publishing date	1990-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/jb.172.8.4529-4535.1990
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Article: L-serine degradation in Escherichia coli K-12: a combination of L-serine, glycine, and leucine used as a source of carbon.

Newman, E B / Walker, C

Journal of bacteriology

1982 Volume 151, Issue 2, Page(s) 777–782

Abstract: Escherichia coli K-12 strain CU1008 cannot use L-serine as the sole carbon source, but it could use ... L-serine as an auxiliary carbon source with glucose, L-alanine, or pyruvate and could derive energy ... from L-serine to support oxygen uptake. CU1008 grew with L-serine if it was also provided with glycine ...

Abstract	Escherichia coli K-12 strain CU1008 cannot use L-serine as the sole carbon source, but it could use L-serine as an auxiliary carbon source with glucose, L-alanine, or pyruvate and could derive energy from L-serine to support oxygen uptake. CU1008 grew with L-serine if it was also provided with glycine and leucine. These may act by increasing the available activity of L-serine deaminase; other explanations are also explored.
MeSH term(s)	Energy Metabolism ; Escherichia coli/metabolism ; Glucose/metabolism ; Glycine/metabolism ; Leucine/metabolism ; Oxygen Consumption ; Serine/metabolism ; Triose-Phosphate Isomerase/metabolism
Chemical Substances	Serine (452VLY9402) ; Triose-Phosphate Isomerase (EC 5.3.1.1) ; Leucine (GMW67QNF9C) ; Glucose (IY9XDZ35W2) ; Glycine (TE7660XO1C)
Language	English
Publishing date	1982-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/jb.151.2.777-782.1982
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Article: L-serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene.

Su, H S / Lang, B F / Newman, E B

Journal of bacteriology

1989 Volume 171, Issue 9, Page(s) 5095–5102

Abstract: A new mutant of Escherichia coli K-12 unable to grow with L-serine, glycine, and L-leucine has been ... isolated by lambda plac Mu insertion and shown to be deficient in L-serine deaminase activity ... sequenced. The evidence is consistent with the hypothesis that sdaA is the structural gene for L-serine ...

Abstract	A new mutant of Escherichia coli K-12 unable to grow with L-serine, glycine, and L-leucine has been isolated by lambda plac Mu insertion and shown to be deficient in L-serine deaminase activity. The corresponding gene, sdaA, has been cloned from a prototrophic strain, and the clone has been characterized and sequenced. The evidence is consistent with the hypothesis that sdaA is the structural gene for L-serine deaminase. However, other possibilities are also considered. No significant homology with previously reported DNA or protein sequences was detected.
MeSH term(s)	Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Coliphages/genetics ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Genes ; Genes, Bacterial ; L-Serine Dehydratase/genetics ; Molecular Sequence Data ; Plasmids ; Restriction Mapping ; Serine/metabolism
Chemical Substances	Serine (452VLY9402) ; L-Serine Dehydratase (EC 4.3.1.17)
Language	English
Publishing date	1989-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/jb.171.9.5095-5102.1989
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Article ; Online: A Systematic Review of Inflammatory Bowel Disease Epidemiology and Health Outcomes in Sexual and Gender Minority Individuals.

Newman, Kira L / Chedid, Victor G / Boden, Elisa K

Gastroenterology

2023 Volume 164, Issue 6, Page(s) 866–871

MeSH term(s)	Humans ; Sexual and Gender Minorities ; Outcome Assessment, Health Care
Language	English
Publishing date	2023-03-05
Publishing country	United States
Document type	Systematic Review ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80112-4
ISSN	1528-0012 ; 0016-5085
ISSN (online)	1528-0012
ISSN	0016-5085
DOI	10.1053/j.gastro.2022.11.048
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