Amino Terminal Sequence of the Tryptophan Synthetase Alpha Chain of
            <i>Serratia marcescens</i>

Li, Shoei-Lung; Drapeau, Gabriel R.; Yanofsky, Charles

doi:10.1128/jb.113.3.1507-1508.1973

Cited by 10 publications

(5 citation statements)

References 8 publications

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“…Acid Sequences Primary sequence analysis of the a-chain of TS has been accomplished for three enteric bacterial species (76,136,137), and partial, amino-terminal sequences are available for two others (133,135). These data are summarized in Fig.…”

Section: Subunit Structure Of Enzymes and Aniinomentioning

confidence: 99%

Gene rearrangements in the evolution of the tryptophan synthetic pathway.

Crawford¹

1975

Bacteriological Reviews

122

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Section: Subunit Structure Of Enzymes and Aniinomentioning

confidence: 99%

Gene rearrangements in the evolution of the tryptophan synthetic pathway.

Crawford¹

1975

Bacteriological Reviews

122

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“…1. The similarity of a chains relative to E. coli had previously been estimated as S. dysenteriae > A. aerogenes > S. typhimurium > S. marcescens > P. putida (8). It is obvious that the B. subtilis sequence (1) shows the greatest divergence from the E. coli sequence.…”

Section: Methodsmentioning

confidence: 99%

“…The complete sequence is known for the subunit from Escherichia coli (4), Salmonella typhimurium (10), and Aerobacter aerogenes (11). The NH,-terminal sequences have been reported for the a chain from Shigella dysenteriae (9), Serratia marcescens (8), and Pseudomonas putida (1). The species mentioned are all gram negative and exhibit only a vegetative life cycle.…”

mentioning

confidence: 99%

Amino-Terminal Sequence of the Tryptophan Synthetase α Chain of Bacillus subtilis

Hoch

1974

J Bacteriol

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“…Studies on the immunological cross-reactivities of the a and 12 subunits of tryptophan synthase from representative species of various genera of the enteric bacteria (7,30,38) and on the immunological relationships of the alkaline phosphatases from the same species (6) show that the enzymes from Serratia have less crossreactivity with the antiserum prepared against the E. coli protein than the corresponding enzymes from the Escherichia, Shigella, Salmonella, Citrobacter, and KlebsiellalEnterobacter group. Furthermore, partial and full primary sequence analysis of the a chain of the tryptophan synthase indicates that the S. marcescens protein is more dissimilar in sequence to the E. coli a chain than are the S. typhimurium, E. aerogenes, and S. dysenteriae a chains (7,13,(22)(23)(24)(25).…”

Section: Value Of Amp For Either the Atcc 15365 Ormentioning

confidence: 99%

Kinetic properties of Serratia marcescens adenosine 5'-diphosphate glucose pyrophosphorylase

Preiss¹,

Crawford²,

Downey³

et al. 1976

J Bacteriol

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The regulatory properties of partially purified adenosine 5'-diphosphate-(ADP) glucose pyrophosphorylase from two Serratia marcescens strains (ATCC 274 and ATCC 15365) have been studied. Slight or negligible activation by fructose-P2, pyridoxal-phosphate, or reduced nicotinamide adenine dinucleotide phosphate (NADPH) was observed. These compounds were previously shown to be potent activators of the ADPglucose pyrophosphorylases from the enterics, Salmonella typhimurium, Enterobacter aerogenes, Enterobacter cloacae, Citrobacter freundii, Escherichia aurescens, Shigella dysenteriae, and Escherichia coli. Phosphoenolpyruvate stimulated the rate of ADPglucose synthesis catalyzed by Serratia ADPglucose pyrophosphorylase about 1.5-to 2-fold but did not affect the So.5 values (concentration of substrate required for 50% maximal stimulation) of the substrates, a-glucose-i-phosphate, and adenosine 5'-triphosphate. Adenosine 5'-monophosphate (AMP), a potent inhibitor of the enteric ADPglucose pyrophosphorylase, is an effective inhibitor of the S. marcescens enzyme. ADP also inhibits but is not as effective as AMP. Activators of the enteric enzyme counteract the inhibition caused by AMP. This is in contrast to what is observed for the S. marcescens enzyme. Neither phosphoenolpyruvate, fructose-diphosphate, pyridoxal-phosphate, NADPH, 3-phosphoglycerate, fructose-6-phosphate, nor pyruvate effect the inhibition caused by AMP. The properties of the S. marcescens HY strain and Serratia liquefaciens ADPglucose pyrophosphorylase were found to be similar to the above two S. marcescens enzynies with respect to activation and inhibition. These observations provide another example where the properties of an enzyme found in the genus Serratia have been found to be different from the properties of the same enzyme present in the enteric genera Escherichia, Salmonella, Shigella, Citrobacter, and Enterobacter. 193 on July 16, 2020 by guest

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Amino Terminal Sequence of the Tryptophan Synthetase Alpha Chain of Serratia marcescens

Abstract: The sequence of the amino terminal 28 residues of the tryptophan synthetase α chain of Serratia marcescens is presented and compared with the related sęquences of α chains of other bacteria.

Cited by 10 publications

References 8 publications

Gene rearrangements in the evolution of the tryptophan synthetic pathway.

Gene rearrangements in the evolution of the tryptophan synthetic pathway.

Amino-Terminal Sequence of the Tryptophan Synthetase α Chain of Bacillus subtilis

Kinetic properties of Serratia marcescens adenosine 5'-diphosphate glucose pyrophosphorylase

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