Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	1 proteins
Enzyme class ^help_outline	EC 1.2.1.60 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
GO Molecular Function ^help_outline	GO:0018480 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity

Reaction participants Show >> << Hide

Name ^help_outline 2-hydroxy-5-carboxymethylmuconate semialdehyde Identifier CHEBI:58030 Charge -2 Formula C8H6O6 InChIKey^help_outline NLXIEJRQAIHYPN-IOBHVTPZSA-L SMILES^help_outline [H]C(=O)C(\CC([O-])=O)=C/C=C(\O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NAD⁺ Identifier CHEBI:57540 (Beilstein: 3868403) ^help_outline Charge -1 Formula C21H26N7O14P2 InChIKey^help_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILES^help_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,207 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O Identifier CHEBI:15377 (CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,418 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline (2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate Identifier CHEBI:47961 (Beilstein: 5874593) ^help_outline Charge -3 Formula C8H5O7 InChIKey^help_outline HJIBROWPWNLWHX-IKENXXAYSA-K SMILES^help_outline O\C(=C/C=C(\CC([O-])=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) ^help_outline Charge -2 Formula C21H27N7O14P2 InChIKey^help_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILES^help_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,136 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,836 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:15681	RHEA:15682	RHEA:15683	RHEA:15684
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	1 proteins	1 proteins
EC numbers ^help_outline	1.2.1.60
Gene Ontology ^help_outline	GO:0018480
KEGG ^help_outline				R04418
MetaCyc ^help_outline		CHMS-DEHYDROGENASE-RXN

Related reactions ^help_outline

More general form(s) of this reaction

RHEA:16185
an aldehyde + NAD⁺ + H₂O = a carboxylate + NADH + 2 H⁺

Publications

Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli.

Alonso J.M., Garrido-Pertierra A.

5-Carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate meta-cleavage pathway has been purified to 96% homogeneity. The native enzyme, which appears to be a tetramer, has an apparent molecular weight of 210000. The purified enzyme shows a narrow pH optimum at pH 7 ... >> More

5-Carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate meta-cleavage pathway has been purified to 96% homogeneity. The native enzyme, which appears to be a tetramer, has an apparent molecular weight of 210000. The purified enzyme shows a narrow pH optimum at pH 7.8 and does not require ions for its catalytic activity. Under standard assay conditions the enzyme acts preferentially with NAD but reduces NADP at 11% of the rate observed for NAD, primarily because of a difference in Km. Apparent Km values are 6.4 micro M for 5-carboxymethyl-2-hydroxymuconic semialdehyde and 52.2 micro M for NAD. << Less

Biochim Biophys Acta 719:165-167(1982) [PubMed] [EuropePMC]
5-Carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenases of Escherichia coli C and Klebsiella pneumoniae M5a1 show very high N-terminal sequence homology.

Fawcett T., Garrido-Pertierra A., Cooper R.A.

5-Carboxymethyl-2-hydroxymuconic semialdehyde (CHMS) dehydrogenase from Escherichia coli C and Klebsiella pneumoniae M5a1 have been purified and some of their properties studied. The apparent Km values for NAD and CHMS were 11.7 +/-1.5 microM and 5.2 +/-1.9 microM, respectively, for the K. pneumon ... >> More

5-Carboxymethyl-2-hydroxymuconic semialdehyde (CHMS) dehydrogenase from Escherichia coli C and Klebsiella pneumoniae M5a1 have been purified and some of their properties studied. The apparent Km values for NAD and CHMS were 11.7 +/-1.5 microM and 5.2 +/-1.9 microM, respectively, for the K. pneumoniae enzyme, and 19.5 +/-2.7 microM and 9.2 +/-1.4 microM, respectively, for the E. coli enzyme. Both enzymes were optimally active at pH 7.5 in sodium phosphate buffer. They had subunit molecular weights of 52,000 (+/-1000) and the native enzymes appeared to be dimers of identical subunits. The first 20 residues of their N-terminal amino acid sequences were 90% homologous. A degenerate oligonucleotide probe constructed to a six amino acid sequence common to both enzymes gave strong hybridization with DNA from E. coli strains B and W as well as with E. coli C and K. pneumoniae but little or no hybridization to DNA from E. coli K12 or Pseudomonas putida. << Less

FEMS Microbiol. Lett. 57:307-311(1989) [PubMed] [EuropePMC]
Kinetic properties of 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase from Escherichia coli.

Alonso J.M., Garrido-Pertierra A.

Kinetic properties of purified 5-carboxymethyl-2-hydroxymuconate semialdehyde (CHMSA) dehydrogenase (EC 1.2.1.-) in the 4-hydroxyphenylacetate meta-cleavage pathway from Escherichia coli have been studied. The temperature--activity relationship for the enzyme from 27 to 45 degrees C showed an Arrh ... >> More

Kinetic properties of purified 5-carboxymethyl-2-hydroxymuconate semialdehyde (CHMSA) dehydrogenase (EC 1.2.1.-) in the 4-hydroxyphenylacetate meta-cleavage pathway from Escherichia coli have been studied. The temperature--activity relationship for the enzyme from 27 to 45 degrees C showed an Arrhenius plot with an inflexion at 36 degrees C. When 5-carboxymethyl-2-hydroxymuconic semialdehyde and NAD were used as variable substrates, the double reciprocal plots were all linear and the lines intersected at one point below the horizontal axis, suggesting that a sequential mechanism is operating. From the replots of intercepts and slopes against reciprocal substrate concentrations were calculated Km (CHMSA) = 9.0 +/- 1.02 microM, Km (NAD) = 29.1 +/-4.65 microM and the value for the dissociation constant of enzyme--NAD complex = 6.3 +/-1.21 microM. ATP and the product of the reaction (NADH) acted as competitive inhibitors of the enzyme with respect to NAD. Apparent Ki values, estimated from Dixon plots, were 25.0 +/- 3.5 and 88.0 +/-22.1 microM for NADH and ATP, respectively. << Less

Biochimie 68:731-737(1986) [PubMed] [EuropePMC]
Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli.

Cooper R.A., Skinner M.A.

Various strains of Escherichia coli (but not strain K-12) were found to grow on 3-hydroxyphenylacetate and 4-hydroxyphenylacetate. Both compounds were catabolized by the same pathway, with 3,4-dihydroxyphenylacetate as a substrate for fission of the benzene nucleus, and with pyruvate and succinate ... >> More

Various strains of Escherichia coli (but not strain K-12) were found to grow on 3-hydroxyphenylacetate and 4-hydroxyphenylacetate. Both compounds were catabolized by the same pathway, with 3,4-dihydroxyphenylacetate as a substrate for fission of the benzene nucleus, and with pyruvate and succinate as products. All the necessay enzymes were demonstrated in cell extracts prepared from induced cells but were essentially absent from uninduced cells. Mutants unable to grow on 3- and 4-hydroxyphenylactetate were defective in particular enzymes of the pathway. The characteristics of certain mutants indicated that either uptake or hydroxylation of 3- and 4-hydroxyphenylacetate may involve a common protein component. E. coli also grew on 3,4-hydroxyphenylacetate, with induction of the enzyme necessary for its degradation but not those for the uptake-hydroxylation of 3- and 4-hydroxyphenylacetate. << Less

J Bacteriol 143:302-306(1980) [PubMed] [EuropePMC]
The catabolism of L-tyrosine by an Arthrobacter sp.

Blakley E.R.

An Arthrobacter sp. metabolizes L-tyrosine by a pathway involving 3,4-dihydroxyphenylacetate as a key intermediate. p-Hydroxyphenylpyruvate is formed from tyrosine by an amino-transferase specifically requiring alpha-ketoglutarate for activity, and is then converted to p-hydroxyphenylacetate by an ... >> More

An Arthrobacter sp. metabolizes L-tyrosine by a pathway involving 3,4-dihydroxyphenylacetate as a key intermediate. p-Hydroxyphenylpyruvate is formed from tyrosine by an amino-transferase specifically requiring alpha-ketoglutarate for activity, and is then converted to p-hydroxyphenylacetate by an oxidative decarboxylation. p-Hydroxyphenylacetaldehyde is not an intermediate in the formation of p-hydroxyphenylacetate. Extracts of the bacterium oxidize 3,4-dihydroxyphenylacetate to delta-carboxymethyl-alpha-hydroxymuconic acid which, when supplemented with 2 mol of diphosphopyridine dinucleotide, results in the production of stoichiometric amounts of succinate and pyruvate. << Less

Can J Microbiol 23:1128-1139(1977) [PubMed] [EuropePMC]

This publication is cited by 1 other entry.
Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli.

Garrido-Peritierra A., Cooper R.A.

The possible involvement of an isomerase in the 4-hydroxyphenylacetate meta-cleavage pathway has been studied. 5-Carboxymethyl-2-hydroxymuconate has been shown to undergo both spontaneous and enzyme-catalysed isomerisation to give 5-carboxymethyl-2-oxo-hex-3-ene-1,5-dioate, a compound with an abso ... >> More

The possible involvement of an isomerase in the 4-hydroxyphenylacetate meta-cleavage pathway has been studied. 5-Carboxymethyl-2-hydroxymuconate has been shown to undergo both spontaneous and enzyme-catalysed isomerisation to give 5-carboxymethyl-2-oxo-hex-3-ene-1,5-dioate, a compound with an absorbance maximum at 246 nm. The latter compound rather than the former is the substrate for a decarboxylase that produces 2-hydroxyhepta-2,4-diene,1,7-dioate. The isomerase and decarboxylase enzymes have been purified to over 90% homogeneity. Mg2+ is required for the decarboxylase reaction but not for the isomerase. << Less

Eur J Biochem 117:581-584(1981) [PubMed] [EuropePMC]

This publication is cited by 4 other entries.

RHEA:15681 2-hydroxy-5-carboxymethylmuconate semialdehyde + NAD(+) + H2O = (2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate + NADH + 2 H(+)

Enzymes

Reaction participants Show >> << Hide

Cross-references

Related reactions help_outline

More general form(s) of this reaction

Publications

Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli.

5-Carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenases of Escherichia coli C and Klebsiella pneumoniae M5a1 show very high N-terminal sequence homology.

Kinetic properties of 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase from Escherichia coli.

Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli.

The catabolism of L-tyrosine by an Arthrobacter sp.

Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli.

Related reactions ^help_outline