DOI: 10.1128/jb.96.5.1512-1518.1968. <scp>l</scp> -Serine Deaminase of <i>Escherichia coli</i>

10.1128/jb.96.5.1512-1518.1968

Crossref journal-article

American Society for Microbiology

Journal of Bacteriology (235)

Abstract

The native l -serine deaminase ( l -serine hydrolyase, deaminating, EC 4.2.1.13) of Escherichia coli K-12, which seems to be a very labile protein, is rather stable in concentrated solution. Dilution rapidly inactivates it, but in the presence of a saturating concentration of l -serine the molecule is protected from inactivation. It is a very specific enzyme; l -serine is the sole substrate with a K m value of 6.60 × 10 −3 m. d -Serine and l -cysteine are competitive inhibitors. Substrate saturation curves of the native enzyme show sigmoid shape, whereas the enzyme liberated from the bacteria in the presence of l -serine exhibits normal Michaelis-Menten kinetics.

Bibliography

AlfÃ¶ldi, L., RaskÃ³, I., & Kerekes, E. (1968). l -Serine Deaminase of Escherichia coli. Journal of Bacteriology, 96(5), 1512â1518.

Authors 3

Lajos Alföldi (first)
István Raskó (additional)
Erzsébet Kerekes (additional)

References 15 Referenced 29

Artman , M. , and J. Markenson . 1958 . Studies on serine and threonine deaminases of Escherichia coli and the action of dihydrostreptomycine thereupon . Enzymologia 19 : 9 - 15 . / Enzymologia / Studies on serine and threonine deaminases of Escherichia coli and the action of dihydrostreptomycine thereupon by Artman M. (1958)
Benziman , M. , R. D. Sagers , and I. C. Gunsalus . 1960 . L-Serine specific dehydrase from Clostridiuwn acidi-urici . J. Bacteriol. 79 : 474 - 479 . (10.1128/JB.79.4.474-479.1960) / J. Bacteriol. / L-Serine specific dehydrase from Clostridiuwn acidi-urici by Benziman M. (1960)
Boyd , W. L. , and H. C. Lichstein . 1955 . The influence of nutrition on the serine and threonine deaminases of microorganisms . J. Bacteriol. 69 : 545 - 548 . (10.1128/JB.69.5.545-548.1955) / J. Bacteriol. / The influence of nutrition on the serine and threonine deaminases of microorganisms by Boyd W. L. (1955)
Bridgeland , E. S. , and K. M. Jones . 1965 . LSerine dehydrase of Arthrobacter globiformis . Biochem. J. 94 : 29 . / Biochem. J. / LSerine dehydrase of Arthrobacter globiformis by Bridgeland E. S. (1965)
Friedemann , T. E. , and G. E. Haugen . 1943 . Pyruvic acid. II. The determination of keto acids in blood and urine . J. Biol. Chem. 147 : 415 - 442 . / J. Biol. Chem. / Pyruvic acid. II. The determination of keto acids in blood and urine by Friedemann T. E. (1943)
Gale , E. F. , and M. Stephenson . 1938 . Factors influencing the activity of DL-serine deaminase in Bacterium coli . Biochem. J. 32 : 392 - 404 . (10.1042/bj0320392) / Biochem. J. / Factors influencing the activity of DL-serine deaminase in Bacterium coli by Gale E. F. (1938)
Goldstein , L. , W. E. Knox , and E. J. Behrman . 1962 . Studies on the nature, inducibility, and assay of the threonine and serine dehydrase activities of rat liver . J. Biol. Chem. 237 : 2855 - 2860 . (10.1016/S0021-9258(18)60240-6) / J. Biol. Chem. / Studies on the nature, inducibility, and assay of the threonine and serine dehydrase activities of rat liver by Goldstein L. (1962)
Lowry , 0. H. , N. J. Rosebrough , A. L. Farr , and R. J. Randall . 1951 . Protein measurement with the Folin phenol reagent . J. Biol. Chem. 193 : 265 - 275 . (10.1016/S0021-9258(19)52451-6) / J. Biol. Chem. / Protein measurement with the Folin phenol reagent by Lowry 0. (1951)
Metzler , D. E. , and E. E. Snell . 1952 . Deamination of serine. II. D-Serine dehydrase, a vitamin B6 enzyme . J. Biol. Chem. 198 : 363 - 373 . / J. Biol. Chem. / Deamination of serine. II. D-Serine dehydrase, a vitamin B6 enzyme by Metzler D. E. (1952)
Monod , J. , J. Wyman , and J. P. Changeux . 1965 . On the nature of allosteric transitions: a plausible model . J. Mol. Biol. 12 : 88 - 118 . (10.1016/S0022-2836(65)80285-6) / J. Mol. Biol. / On the nature of allosteric transitions: a plausible model by Monod J. (1965)
Nagabhushanam , A. , and D. M. Greenberg . 1965 . Isolation and properties of a homogeneous preparation of cystathione synthetase-Lserine and L-threonine dehydratase . J. Biol. Chem. 240 : 3002 - 3008 . (10.1016/S0021-9258(18)97278-9) / J. Biol. Chem. / Isolation and properties of a homogeneous preparation of cystathione synthetase-Lserine and L-threonine dehydratase by Nagabhushanam A. (1965)
Pardee , A. B. , and L. S. Prestidge . 1955 . Induced formation of serine and threonine deaminases by Escherichia coli . J. Bacteriol. 70 : 667 - 674 . (10.1128/JB.70.6.667-674.1955) / J. Bacteriol. / Induced formation of serine and threonine deaminases by Escherichia coli by Pardee A. B. (1955)
Szentirmai , A. , and I. Horvath . 1962 . L-Serine deaminase from Streptomyces rimosus . Acta Microbiol. Acad. Sci. Hung. 9 : 23 - 30 . / Acta Microbiol. Acad. Sci. Hung. / L-Serine deaminase from Streptomyces rimosus by Szentirmai A. (1962)
Wood , W. A. , and I. C. Gunsalus . 1949 . Serine and threonine deaminases of Escherichia coli: activators for a cell-free enzyme . J. Biol. Chem. 181 : 171 - 182 . (10.1016/S0021-9258(18)56638-2) / J. Biol. Chem. / Serine and threonine deaminases of Escherichia coli: activators for a cell-free enzyme by Wood W. A. (1949)
Yanofsky , C. , and J. L. Reissig . 1953 . L-Serine dehydrase of Neurospora . J. Biol. Chem. 202 : 567 - 577 . (10.1016/S0021-9258(18)66170-8) / J. Biol. Chem. / L-Serine dehydrase of Neurospora by Yanofsky C. (1953)

Dates

Type	When
Created	5 years, 7 months ago (Jan. 4, 2020, 9:11 p.m.)
Deposited	4 years, 1 month ago (July 29, 2021, 12:49 p.m.)
Indexed	1 year, 4 months ago (April 29, 2024, 11:13 a.m.)
Issued	56 years, 9 months ago (Nov. 1, 1968)
Published	56 years, 9 months ago (Nov. 1, 1968)
Published Print	56 years, 9 months ago (Nov. 1, 1968)

Funders 0

None

BibTeX

@article{Alf_ldi_1968, title={<scp>l</scp> -Serine Deaminase of Escherichia coli}, volume={96}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.96.5.1512-1518.1968}, DOI={10.1128/jb.96.5.1512-1518.1968}, number={5}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Alföldi, Lajos and Raskó, István and Kerekes, Erzsébet}, year={1968}, month=nov, pages={1512–1518} }

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  "abstract": "<jats:p>\n            The native\n            <jats:sc>l</jats:sc>\n            -serine deaminase (\n            <jats:sc>l</jats:sc>\n            -serine hydrolyase, deaminating, EC 4.2.1.13) of\n            <jats:italic>Escherichia coli</jats:italic>\n            K-12, which seems to be a very labile protein, is rather stable in concentrated solution. Dilution rapidly inactivates it, but in the presence of a saturating concentration of\n            <jats:sc>l</jats:sc>\n            -serine the molecule is protected from inactivation. It is a very specific enzyme;\n            <jats:sc>l</jats:sc>\n            -serine is the sole substrate with a\n            <jats:italic>K</jats:italic>\n            <jats:sub>m</jats:sub>\n            value of 6.60 \u00d7 10\n            <jats:sup>\u22123</jats:sup>\n            <jats:sc>m. d</jats:sc>\n            -Serine and\n            <jats:sc>l</jats:sc>\n            -cysteine are competitive inhibitors. Substrate saturation curves of the native enzyme show sigmoid shape, whereas the enzyme liberated from the bacteria in the presence of\n            <jats:sc>l</jats:sc>\n            -serine exhibits normal Michaelis-Menten kinetics.\n          </jats:p>",
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