1995
DOI: 10.1016/0378-1119(95)00596-8
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Sequence of the Escherichia coli C homoprotocatechuic acid degradative operon completed with that of the 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase-encoding gene (hpcH)

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Cited by 11 publications
(8 citation statements)
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“…1) (250,303). Unlike the situation mentioned above for the aromatic hydratases, there is no striking identity between HHED aldolase (262 aa) and most of the aldolases of catechol meta-fission pathways.…”
Section: Hpc Meta Cleavage Dehydrogenative Routementioning
confidence: 75%
See 1 more Smart Citation
“…1) (250,303). Unlike the situation mentioned above for the aromatic hydratases, there is no striking identity between HHED aldolase (262 aa) and most of the aldolases of catechol meta-fission pathways.…”
Section: Hpc Meta Cleavage Dehydrogenative Routementioning
confidence: 75%
“…1). An aldol cleavage reaction that resembles that on HHED is found in the catabolism of glucarate and galactarate, and therefore the YhaF protein has been suggested to be the ␣-dehydro-␤-deoxy-D-glucarate aldolase that produces pyruvate and tartronic semialdehyde (151,303), with the YhaU protein being a putative glucarate transporter (223).…”
Section: Hpc Meta Cleavage Dehydrogenative Routementioning
confidence: 99%
“…An interesting observation is that a number of carbohydrate metabolism genes are down regulated in the stationary phase comparison: glycolate oxidase (glcD) in the glyoxylate cycle, glyceraldehyde-3-phosphate dehydrogenase (gap) and fructose-1,6-bisphosphatase (fbp) in the glycolysis pathway, ribose 5-phosphate isomerase in the pentose-phosphate pathway, and HPCH/HPAI aldolase in the homoprotocatechuic acid (HPC) pathway that converts peripheral metabolites into intermediates of central metabolism (Stringfellow et al 1995). Of particular interest are the two glycolysis pathway genes, which may indicate the use of polyglucose in the lactate depleted cells.…”
Section: Resultsmentioning
confidence: 99%
“…Comparison of ThnF to other aldolases in the databases showed similarity to aldolases involved in degradation of homoprotocatechuate and 4-hydroxyphenylacetate, which use 2,4-dihydroxyhept-2-ene-1,7-dioic acid as the substrate (17,29); aldolases potentially involved in degradation of ethylbenzene and biphenyls (14,18); and other known or presumed aldolases from different bacteria. Interestingly, BLAST analysis did not reveal significant homology of ThnF to other aldolases involved in the degradation of aromatic compounds, which use 4-hydroxy-2-oxovalerate as the substrate.…”
Section: Resultsmentioning
confidence: 94%
“…More distantly related hydratases and aldolases involved in biodegradation of homoprotocatechuate metabolize a larger dicarboxylic intermediate, 2-oxohepta-3-enedioic acid. In this case, the substrate of the hydratase appears to be the keto tautomer (19), which is hydrated to 2,4-dihydroxyhepta-2-enedioic acid, the substrate of the aldolase, yielding pyruvate and succinic semialdehyde (17,21,29).…”
mentioning
confidence: 99%