Purification and Characterization of Aminoimidazole Ribonucleotide Synthetase from Escherichia coli

J. L. Schrimsher; F. J. Schendel; J. Stubb; J. M. Smith

doi:10.1021/bi00363a028

Purification and Characterization of Aminoimidazole Ribonucleotide Synthetase from Escherichia coli

J. L. Schrimsher
, F. J. Schendel
, J. Stubb
, J. M. Smith

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

45 Scopus citations

Abstract

Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent ho-mogeneity from Escherichia coli which contains a multicopy plasmid containing the purM, AIR synthetase, gene. The protein is a dimer composed of two identical subunits of M_r38 500. The N-terminal sequence, amino acid composition, and steady-state kinetics of the protein have been determined. AIR synthetase has been shown to catalyze the transfer of the formyl oxygen of [¹⁸0]formylglycinamide ribonucleotide to P_i.

Original language	English (US)
Pages (from-to)	4366-4371
Number of pages	6
Journal	Biochemistry
Volume	25
Issue number	15
DOIs	https://doi.org/10.1021/bi00363a028
State	Published - Jul 1986
Externally published	Yes

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10.1021/bi00363a028

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title = "Purification and Characterization of Aminoimidazole Ribonucleotide Synthetase from Escherichia coli",

abstract = "Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent ho-mogeneity from Escherichia coli which contains a multicopy plasmid containing the purM, AIR synthetase, gene. The protein is a dimer composed of two identical subunits of Mr38 500. The N-terminal sequence, amino acid composition, and steady-state kinetics of the protein have been determined. AIR synthetase has been shown to catalyze the transfer of the formyl oxygen of [180]formylglycinamide ribonucleotide to Pi.",

author = "Schrimsher, \{J. L.\} and Schendel, \{F. J.\} and J. Stubb and Smith, \{J. M.\}",

year = "1986",

month = jul,

doi = "10.1021/bi00363a028",

language = "English (US)",

volume = "25",

pages = "4366--4371",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "15",

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T1 - Purification and Characterization of Aminoimidazole Ribonucleotide Synthetase from Escherichia coli

AU - Schrimsher, J. L.

AU - Schendel, F. J.

AU - Stubb, J.

AU - Smith, J. M.

PY - 1986/7

Y1 - 1986/7

N2 - Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent ho-mogeneity from Escherichia coli which contains a multicopy plasmid containing the purM, AIR synthetase, gene. The protein is a dimer composed of two identical subunits of Mr38 500. The N-terminal sequence, amino acid composition, and steady-state kinetics of the protein have been determined. AIR synthetase has been shown to catalyze the transfer of the formyl oxygen of [180]formylglycinamide ribonucleotide to Pi.

AB - Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent ho-mogeneity from Escherichia coli which contains a multicopy plasmid containing the purM, AIR synthetase, gene. The protein is a dimer composed of two identical subunits of Mr38 500. The N-terminal sequence, amino acid composition, and steady-state kinetics of the protein have been determined. AIR synthetase has been shown to catalyze the transfer of the formyl oxygen of [180]formylglycinamide ribonucleotide to Pi.

UR - https://www.scopus.com/pages/publications/0023058912

UR - https://www.scopus.com/pages/publications/0023058912#tab=citedBy

U2 - 10.1021/bi00363a028

DO - 10.1021/bi00363a028

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AN - SCOPUS:0023058912

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SP - 4366

EP - 4371

JO - Biochemistry

JF - Biochemistry

IS - 15

ER -

Purification and Characterization of Aminoimidazole Ribonucleotide Synthetase from Escherichia coli

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