An N-methyl glutamate dehydrogenase from Pseudomonas M.A

Louis B. Hersh; Julian A. Peterson; Aubrey A. Thompson

doi:10.1016/0003-9861(71)90016-6

An N-methyl glutamate dehydrogenase from Pseudomonas M.A

Louis B. Hersh, Julian A. Peterson, Aubrey A. Thompson

Research output: Contribution to journal › Article › peer-review

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Abstract

Methylamine-induced cells of Pseudomonas MA (ATCC No. 23819) contain a particulate enzyme system which catalyzes the reaction: 2 N-methyl l-glutamate + O₂ → 2 l-glutamate + 2 formaldehyde + (H₂O). The stoichiometry of this reaction (2 moles N-methyl l-glutamate utilized per mole of oxygen) suggests that the enzyme is a dehydrogenase. During the oxidation of N-methyl l-glutamate, cytochromes b and c are enzymatically reduced, supporting the conclusion that the enzyme is a respiratory chain-linked dehydrogenase. It is proposed that the function of this enzyme is to activate the methyl group of N-methyl l-glutamate so that it may be further metabolized by this microorganism.

Original language	English
Pages (from-to)	115-120
Number of pages	6
Journal	Archives of Biochemistry and Biophysics
Volume	145
Issue number	1
DOIs	https://doi.org/10.1016/0003-9861(71)90016-6
State	Published - Jul 1971

Bibliographical note

Funding Information:
1 Support,ed in part by Research 13443 to L. B. H. and Research Grant J. A. P. from the National Institutes and by Research Grant I-391 to L. search Grant to J. A. P. from Welch Foundation. 2 Pollock, unpublished

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "An N-methyl glutamate dehydrogenase from Pseudomonas M.A",

abstract = "Methylamine-induced cells of Pseudomonas MA (ATCC No. 23819) contain a particulate enzyme system which catalyzes the reaction: 2 N-methyl l-glutamate + O2 → 2 l-glutamate + 2 formaldehyde + (H2O). The stoichiometry of this reaction (2 moles N-methyl l-glutamate utilized per mole of oxygen) suggests that the enzyme is a dehydrogenase. During the oxidation of N-methyl l-glutamate, cytochromes b and c are enzymatically reduced, supporting the conclusion that the enzyme is a respiratory chain-linked dehydrogenase. It is proposed that the function of this enzyme is to activate the methyl group of N-methyl l-glutamate so that it may be further metabolized by this microorganism.",

author = "Hersh, {Louis B.} and Peterson, {Julian A.} and Thompson, {Aubrey A.}",

note = "Funding Information: 1 Support,ed in part by Research 13443 to L. B. H. and Research Grant J. A. P. from the National Institutes and by Research Grant I-391 to L. search Grant to J. A. P. from Welch Foundation. 2 Pollock, unpublished",

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T1 - An N-methyl glutamate dehydrogenase from Pseudomonas M.A

AU - Hersh, Louis B.

AU - Peterson, Julian A.

AU - Thompson, Aubrey A.

N1 - Funding Information: 1 Support,ed in part by Research 13443 to L. B. H. and Research Grant J. A. P. from the National Institutes and by Research Grant I-391 to L. search Grant to J. A. P. from Welch Foundation. 2 Pollock, unpublished

PY - 1971/7

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N2 - Methylamine-induced cells of Pseudomonas MA (ATCC No. 23819) contain a particulate enzyme system which catalyzes the reaction: 2 N-methyl l-glutamate + O2 → 2 l-glutamate + 2 formaldehyde + (H2O). The stoichiometry of this reaction (2 moles N-methyl l-glutamate utilized per mole of oxygen) suggests that the enzyme is a dehydrogenase. During the oxidation of N-methyl l-glutamate, cytochromes b and c are enzymatically reduced, supporting the conclusion that the enzyme is a respiratory chain-linked dehydrogenase. It is proposed that the function of this enzyme is to activate the methyl group of N-methyl l-glutamate so that it may be further metabolized by this microorganism.

AB - Methylamine-induced cells of Pseudomonas MA (ATCC No. 23819) contain a particulate enzyme system which catalyzes the reaction: 2 N-methyl l-glutamate + O2 → 2 l-glutamate + 2 formaldehyde + (H2O). The stoichiometry of this reaction (2 moles N-methyl l-glutamate utilized per mole of oxygen) suggests that the enzyme is a dehydrogenase. During the oxidation of N-methyl l-glutamate, cytochromes b and c are enzymatically reduced, supporting the conclusion that the enzyme is a respiratory chain-linked dehydrogenase. It is proposed that the function of this enzyme is to activate the methyl group of N-methyl l-glutamate so that it may be further metabolized by this microorganism.

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An N-methyl glutamate dehydrogenase from Pseudomonas M.A

Abstract

Bibliographical note

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