Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli

Nobelmann, Barbara; Lengeler, Joseph W.

doi:10.1016/0167-4781(95)00053-j

Cited by 25 publications

(21 citation statements)

References 13 publications

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“…The data presented here and in a recent study (Nobelmann & Lengeler, 1995) suggest that two distinct but otherwise homologous tagatose-l,6-bisphosphate aldolases, GatY and AgaY, are encoded within the E. coli gat and aga operons which map on the chromosome at 46.7 and 70.5 min, respectively. An early study showed that a temperature-sensitive ketose bisphosphate aldolase, encoded by the kba gene within the 71 min region, rather than GatY, assumes the role of tagatose 1,6-bisphosphate cleavage in galactitol metabolism (Lengeler, 1977).…”

Section: Discussionmentioning

confidence: 94%

“…The PTS proteins of the Enzyme IIAga complex (IIA, IIB, IIB', IIC, IIC' and IID) proved to be homologous to the previously established ' splinter' group of Enzymes I1 of the PTS (Reizer etal., 1991b), which includes the mannose Enzyme I1 of E. coli, the fructose Enzyme I1 of B. szibtilis and the recently sequenced sorbose Enzyme I1 of K. pnezimoniae (Nobelmann & Lengeler, 1995 ; Wehmeier e t a/., 1995). These enzyme complexes exhibit little sequence similarity with other sequenced Enzyme I1 proteins of the PTS which comprise the major class of the PTS permeases.…”

Section: Discussionmentioning

confidence: 99%

“…1) proved to be homologous to the protein encoded by gatZ, a functionally unidentified ORF (ORF378) in the galactitol (gat) operon (Nobelmann & Lengeler, 1995). These two proteins exhibit 53 % identity in 376 residues (comparison score of 131 SD).…”

Section: Agaz (Orf 0426)mentioning

confidence: 99%

“…Finally, the three proteins, AgaY(Eco), GatY(Eco) and FBA(Bsu), comprise the third, somewhat loose cluster. Because of the occurrence of GatY in the galactitol operon which encodes ketose bisphosphate aldolase (Nobelmann & Lengeler, 1995), we suggest that GatY, as well as AgaY are tagatose-l,6-bisphosphate aldolases (see Discussion).…”

Section: Fba(cg1) 256mentioning

confidence: 99%

“…pombe (Mutoh & Hayashi, 1994), E. coli , Coryne. glutamicum (von der Osten etal., 1989) and B. subtilis (putative) (Trach et al, 1988;Mitchell etal, 1992), respectively; GatY (Eco) and AgaY (Eco), putative tagatose-1,6-bisphosphate aldolases that are encoded in the gat (Nobelmann & Lengeler, 1995) and aga operons of E. coli (GenBank accession no. U18997), respectively.…”

Section: Agay (Orf 0286)mentioning

confidence: 99%

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Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli

et al. 1996

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~~We have analysed a gene cluster in the 674-769 min region of the Escherichia coli chromosome, revealed by recent systematic genome sequencing. The genes within this cluster include: (1) five genes encoding homologues of the E. coli mannose permease of the phosphotransferase system (IIB, IIB', IIC, IIC' and IID) ; (2) genes encoding a putative N-acetylgalactosamine 6-phosphate metabolic pathway including (a) a deacetylase, (b) an isomerizing deaminase, (c) a putative carbohydrate kinase, and (d) an aldolase; and (3) a transcriptional regulatory protein homologous to members of the DeoR family. Evidence is presented suggesting that the aldolase-encoding gene within this cluster is the previously designated kbe gene that encodes tagatose-1,6-bisphosphate aldolase. These proteins and a novel IIAwn-like protein encoded in the 2-01 min region are characterized with respect to their sequence similarities and phylogenetic relationships with other homologous proteins. A pathway for the metabolism of N-acetylgalactosamine biochemically similar to that for the metabolism of N-acetylglucosamine is proposed.

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Section: Agaz (Orf 0426)mentioning

confidence: 99%

Section: Fba(cg1) 256mentioning

confidence: 99%

Section: Agay (Orf 0286)mentioning

confidence: 99%

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Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli

et al. 1996

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pT3.2I, the Smallest Plasmid of Thiobacillus T3.2

Aparicio

Lorenzo

Perera

2000

Plasmid

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Beneficial knockouts in Escherichia coli for producing hydrogen from glycerol

Tran

Maeda

Sánchez-Torres

et al. 2015

Appl Microbiol Biotechnol

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Glycerol is an inexpensive and abundant source for biofuel production on a large scale. Escherichia coli is a robust bacterium for producing hydrogen; however, its hydrogen productivity from glycerol is low. In this study, we conducted random transposon mutagenesis to identify uncharacterized genes whose inactivation is beneficial for hydrogen production from glycerol. Through screening, four mutant strains were found that are able to have from 1.3- to 1.6-fold higher hydrogen productivity (μmol H2/mg protein) than that of their parent strain (p < 0.05). These mutations were identified as aroM, gatZ, ycgR, and yfgI. The hydrogen yield (mol H2/mol glycerol consumed) of the aroM, gatZ, ycgR, and yfgI strains was 1.7-, 1.4-, 2.4-, and 2.1-fold higher than that of their parent strain, respectively. Moreover, a single disruption in these genes resulted in a faster cell growth and glycerol consumption under anaerobic conditions. In E. coli, AroM is predicted to be involved in the shikimate pathway, GatZ is tagatose-1,6-bisphosphate aldolase 2 which converts dihydroxyacetone phosphate to 1,6-biphosphate, and YcgR acts as a molecular brake limiting the swimming speed and ATP consumption. So far, the function of YfgI in general and in hydrogen production in particular remains unknown.

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Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli

Cited by 25 publications

References 13 publications

Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli

Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli

pT3.2I, the Smallest Plasmid of Thiobacillus T3.2

Beneficial knockouts in Escherichia coli for producing hydrogen from glycerol

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