ExplorEnz: EC 1*

Displaying entries 601-650 of 2549.

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1.2.1.32

Accepted name:

aminomuconate-semialdehyde dehydrogenase

Reaction:

2-aminomuconate 6-semialdehyde + NAD⁺ + H₂O = 2-aminomuconate + NADH + 2 H⁺

For diagram of the later stages of tryptophan catabolism, click here

Other name(s):

2-aminomuconate semialdehyde dehydrogenase; 2-hydroxymuconic acid semialdehyde dehydrogenase; 2-hydroxymuconate semialdehyde dehydrogenase; α-aminomuconic ε-semialdehyde dehydrogenase; α-hydroxymuconic ε-semialdehyde dehydrogenase; 2-hydroxymuconic semialdehyde dehydrogenase

Systematic name:

2-aminomuconate-6-semialdehyde:NAD⁺ 6-oxidoreductase

Comments:

Also acts on 2-hydroxymuconate semialdehyde.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37250-95-6

References:

Ichiyama, A., Nakamura, S., Kawai, H., Honjo, T., Nishizuka, Y., Hayaishi, O. and Senoh, S. Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J. Biol. Chem. 240 (1965) 740–749. [PMID: 14275130]

[EC 1.2.1.32 created 1972]

1.2.1.33

Accepted name:

(R)-dehydropantoate dehydrogenase

Reaction:

(R)-4-dehydropantoate + NAD⁺ + H₂O = (R)-3,3-dimethylmalate + NADH + 2 H⁺

For diagram of pantothenate catabolism, click here

Other name(s):

D-aldopantoate dehydrogenase; D-2-hydroxy-3,3-dimethyl-3-formylpropionate:diphosphopyridine nucleotide (DPN⁺) oxidoreductase

Systematic name:

(R)-4-dehydropantoate:NAD⁺ 4-oxidoreductase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-96-7

References:

1.	Magee, P.T. and Snell, E.E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to α-ketoisovalerate. Biochemistry 5 (1966) 409–416. [PMID: 4287371]

[EC 1.2.1.33 created 1972]

1.2.1.34

Transferred entry:

D-mannonate dehydrogenase (NAD(P)⁺). Now EC 1.1.1.131, mannuronate reductase

[EC 1.2.1.34 created 1972, deleted 1983 [transferred to EC 1.1.1.180, deleted 1984]]

1.2.1.35

Transferred entry:

uronate dehydrogenase. Now EC 1.1.1.203, uronate dehydrogenase

[EC 1.2.1.35 created 1972, deleted 1984]

1.2.1.36

Accepted name:

retinal dehydrogenase

Reaction:

retinal + NAD⁺ + H₂O = retinoate + NADH + 2 H⁺

For diagram of biosynthesis of retinal and derivatives, click here

Other name(s):

cytosolic retinal dehydrogenase

Systematic name:

retinal:NAD⁺ oxidoreductase

Comments:

A metalloflavoprotein (FAD). Acts on both the 11-trans- and 13-cis-forms of retinal.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37250-99-0

References:

1.	Moffa, D.J., Lotspeich, F.J. and Krause, R.F. Preparation and properties of retinal-oxidizing enzyme from rat intestinal mucosa. J. Biol. Chem. 245 (1970) 439–447. [PMID: 4312676]

[EC 1.2.1.36 created 1972]

1.2.1.37

Transferred entry:

xanthine dehydrogenase. Now EC 1.17.1.4, xanthine dehydrogenase

[EC 1.2.1.37 created 1972, deleted 1984]

1.2.1.38

Accepted name:

N-acetyl-γ-glutamyl-phosphate reductase

Reaction:

N-acetyl-L-glutamate 5-semialdehyde + NADP⁺ + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH + H⁺

For diagram of ornithine biosynthesis, click here

Other name(s):

reductase, acetyl-γ-glutamyl phosphate; N-acetylglutamate 5-semialdehyde dehydrogenase; N-acetylglutamic γ-semialdehyde dehydrogenase; N-acetyl-L-glutamate γ-semialdehyde:NADP⁺ oxidoreductase (phosphorylating)

Systematic name:

N-acetyl-L-glutamate-5-semialdehyde:NADP⁺ 5-oxidoreductase (phosphorylating)

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37251-00-6

References:

1.	Baich, A. and Vogel, H.J. N-Acetyl-γ-glutamokinase and N-acetylglutamic γ-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli. Biochem. Biophys. Res. Commun. 7 (1962) 491–496. [PMID: 13863980]
2.	Glansdorff, N. and Sand, G. Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12. Biochim. Biophys. Acta 108 (1965) 308–311. [PMID: 5325238]

[EC 1.2.1.38 created 1972]

1.2.1.39

Accepted name:

phenylacetaldehyde dehydrogenase

Reaction:

phenylacetaldehyde + NAD⁺ + H₂O = phenylacetate + NADH + 2 H⁺

Systematic name:

phenylacetaldehyde:NAD⁺ oxidoreductase

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 58943-37-6

References:

1.	Fujioka, M., Morino, Y. and Wada, H. Metabolism of phenylalanine (Achromobacter eurydice). III. Phenylacetaldehyde dehydrogenase. Methods Enzymol. 17A (1970) 593–596.

[EC 1.2.1.39 created 1976]

1.2.1.40

Deleted entry:

3α,7α,12α-trihydroxycholestan-26-al 26-oxidoreductase. The activity is part of EC 1.14.13.15, cholestanetriol 26-monooxygenase

[EC 1.2.1.40 created 1976, deleted 2012]

1.2.1.41

Accepted name:

glutamate-5-semialdehyde dehydrogenase

Reaction:

L-glutamate 5-semialdehyde + phosphate + NADP⁺ = L-glutamyl 5-phosphate + NADPH + H⁺

For diagram of proline biosynthesis, click here

Other name(s):

β-glutamylphosphate reductase; γ-glutamyl phosphate reductase; β-glutamylphosphate reductase; glutamate semialdehyde dehydrogenase; glutamate-γ-semialdehyde dehydrogenase

Systematic name:

L-glutamate-5-semialdehyde:NADP⁺ 5-oxidoreductase (phosphorylating)

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 54596-29-1

References:

1.	Baich, A. The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate-semialdehyde dehydrogenase (NADP), the second enzyme in the pathway. Biochim. Biophys. Acta 244 (1971) 129–134. [DOI] [PMID: 4399189]

[EC 1.2.1.41 created 1976]

1.2.1.42

Accepted name:

hexadecanal dehydrogenase (acylating)

Reaction:

hexadecanal + CoA + NAD⁺ = hexadecanoyl-CoA + NADH + H⁺

Other name(s):

fatty acyl-CoA reductase

Systematic name:

hexadecanal:NAD⁺ oxidoreductase (CoA-acylating)

Comments:

Also acts, more slowly, on octadecanoyl-CoA.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 72561-01-4

References:

1.	Johnson, R.C. and Gilbertson, J.R. Isolation, characterization, and partial purification of a fatty acyl coenzyme A reductase from bovine cardiac muscle. J. Biol. Chem. 247 (1972) 6991–6998. [PMID: 4343165]

[EC 1.2.1.42 created 1978]

1.2.1.43

Transferred entry:

formate dehydrogenase (NADP⁺). Now EC 1.17.1.10, formate dehydrogenase (NADP⁺)

[EC 1.2.1.43 created 1978, deleted 2017]

1.2.1.44

Accepted name:

cinnamoyl-CoA reductase

Reaction:

cinnamaldehyde + CoA + NADP⁺ = cinnamoyl-CoA + NADPH + H⁺

Other name(s):

feruloyl-CoA reductase; cinnamoyl-coenzyme A reductase; ferulyl-CoA reductase; feruloyl coenzyme A reductase; p-hydroxycinnamoyl coenzyme A reductase; cinnamoyl-CoA:NADPH reductase

Systematic name:

cinnamaldehyde:NADP⁺ oxidoreductase (CoA-cinnamoylating)

Comments:

Acts also on a number of substituted cinnamoyl esters of coenzyme A.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 59929-39-4

References:

1.	Gross, G.G. and Kreiten, W. Reduction of coenzyme A thioesters of cinnamic acids with an enzyme preparation from lignifying tissue of Forsythia. FEBS Lett. 54 (1975) 259–262. [DOI] [PMID: 236926]
2.	Sarni, F., Grand, C. and Baudet, A.M. Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana). Eur. J. Biochem. 139 (1984) 259–265. [DOI] [PMID: 6365550]
3.	Wengenmayer, H., Ebel, J. and Grisebach, H. Enzymic synthesis of lignin precursors. Purification and properties of a cinnamoyl-CoA: NADPH reductase from cell suspension cultures of soybean (Glycinemax). Eur. J. Biochem. 65 (1976) 529–536. [DOI] [PMID: 7454]

[EC 1.2.1.44 created 1978]

1.2.1.45

Transferred entry:

4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase. Now EC 1.1.1.312, 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase.

[EC 1.2.1.45 created 1978, deleted 2011]

1.2.1.46

Accepted name:

formaldehyde dehydrogenase

Reaction:

formaldehyde + NAD⁺ + H₂O = formate + NADH + 2 H⁺

Other name(s):

NAD-linked formaldehyde dehydrogenase; NAD-dependent formaldehyde dehydrogenase

Systematic name:

formaldehyde:NAD⁺ oxidoreductase

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9028-84-6

References:

1.	Hohnloser, W., Osswald, B. and Lingens, F. Enzymological aspects of caffeine demethylation and formaldehyde oxidation by Pseudomonas putida C1. Hoppe-Seyler's Z. Physiol. Chem. 361 (1980) 1763–1766. [PMID: 7461603]

[EC 1.2.1.46 created 1982]

1.2.1.47

Accepted name:

4-trimethylammoniobutyraldehyde dehydrogenase

Reaction:

4-trimethylammoniobutanal + NAD⁺ + H₂O = 4-trimethylammoniobutanoate + NADH + 2 H⁺

Other name(s):

4-trimethylaminobutyraldehyde dehydrogenase; 4-N-trimethylaminobutyraldehyde dehydrogenase

Systematic name:

4-trimethylammoniobutanal:NAD⁺ 1-oxidoreductase

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 73361-01-0

References:

1.	Rebouche, C.J. and Engel, A.G. Tissue distribution of carnitine biosynthetic enzymes in man. Biochim. Biophys. Acta 630 (1980) 22–29. [DOI] [PMID: 6770910]

[EC 1.2.1.47 created 1983]

1.2.1.48

Accepted name:

long-chain-aldehyde dehydrogenase

Reaction:

a long-chain aldehyde + NAD⁺ + H₂O = a long-chain carboxylate + NADH + 2 H⁺

Other name(s):

long-chain aliphatic aldehyde dehydrogenase; long-chain fatty aldehyde dehydrogenase; fatty aldehyde:NAD⁺ oxidoreductase

Systematic name:

long-chain-aldehyde:NAD⁺ oxidoreductase

Comments:

The best substrate is dodecylaldehyde.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 59298-89-4

References:

1.	Le Beault, J.M., Roche, B., Duvnjak, Z. and Azoulay, E. Alcool- et aldéhyde-déshydrogénases particulaires de Candida tropicalis cultivé sur hydrocarbures. Biochim. Biophys. Acta 220 (1970) 373–385. [DOI] [PMID: 5499619]
2.	Moreau, R.A. and Huang, A.H.C. Oxidation of fatty alcohol in the cotyledons of jojoba seedlings. Arch. Biochem. Biophys. 194 (1979) 422–430. [DOI] [PMID: 36040]
3.	Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813.

[EC 1.2.1.48 created 1984]

1.2.1.49

Accepted name:

2-oxoaldehyde dehydrogenase (NADP⁺)

Reaction:

a 2-oxoaldehyde + NADP⁺ + H₂O = a 2-oxo carboxylate + NADPH + H⁺

Other name(s):

α-ketoaldehyde dehydrogenase; methylglyoxal dehydrogenase; NADP⁺-linked α-ketoaldehyde dehydrogenase; 2-ketoaldehyde dehydrogenase; NADP⁺-dependent α-ketoaldehyde dehydrogenase

Systematic name:

2-oxoaldehyde:NADP⁺ 2-oxidoreductase

Comments:

Not identical with EC 1.2.1.23 2-oxoaldehyde dehydrogenase (NAD⁺).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83588-97-0, 97162-76-0

References:

1.	Ray, M. and Ray, S. On the interaction of nucleotides and glycolytic intermediates with NAD-linked α-ketoaldehyde dehydrogenase. J. Biol. Chem. 257 (1982) 10571–10574. [PMID: 7107626]
2.	Ray, S. and Ray, M. Purification and characterization of NAD and NADP-linked α-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate. J. Biol. Chem. 257 (1982) 10566–10570. [PMID: 7107625]

[EC 1.2.1.49 created 1986]

1.2.1.50

Accepted name:

long-chain acyl-protein thioester reductase

Reaction:

a long-chain aldehyde + [protein]-L-cysteine + NADP⁺ = a [protein]-S-(long-chain fatty acyl)-L-cysteine + NADPH + H⁺

Other name(s):

luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP⁺ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase

Systematic name:

long-chain-aldehyde:NADP⁺ oxidoreductase (protein thioester-forming)

Comments:

Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 50936-56-6

References:

1.	Riendeau, D., Rodrigues, A. and Meighen, E. Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex. J. Biol. Chem. 257 (1982) 6908–6915. [PMID: 7085612]
2.	Wall, L. and Meighen, E.A. Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum. Biochemistry 25 (1986) 4315–4321.
3.	Lin, J.W., Chao, Y.F. and Weng, S.F. Nucleotide sequence of the luxC gene encoding fatty acid reductase of the lux operon from Photobacterium leiognathi. Biochem. Biophys. Res. Commun. 191 (1993) 314–318. [DOI] [PMID: 8447834]

[EC 1.2.1.50 created 1986, modified 2016]

1.2.1.51

Accepted name:

pyruvate dehydrogenase (NADP⁺)

Reaction:

pyruvate + CoA + NADP⁺ = acetyl-CoA + CO₂ + NADPH

Glossary:

methyl viologen = 1,1′-dimethyl-4,4′-bipyridine-1,1′-diium

Systematic name:

pyruvate:NADP⁺ 2-oxidoreductase (CoA-acetylating)

Comments:

The Euglena enzyme can also use FAD or methyl viologen as acceptor, more slowly. The enzyme is inhibited by oxygen.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 93389-35-6

References:

1.	Inui, H., Miyatake, K., Nakano, Y. and Kitaoka, S. Occurrence of oxygen-sensitive, NADP +-dependent pyruvate dehydrogenase in mitochondria of Euglena gracilis. J. Biochem. (Tokyo) 96 (1984) 931–934. [PMID: 6438078]
2.	Inui, H., Ono, K., Miyatake, K., Nakano, Y. and Kitaoka, S. Purification and characterization of pyruvate:NADP⁺ oxidoreductase in Euglena gracilis. J. Biol. Chem. 262 (1987) 9130–9135. [PMID: 3110154]

[EC 1.2.1.51 created 1989]

1.2.1.52

Accepted name:

oxoglutarate dehydrogenase (NADP⁺)

Reaction:

2-oxoglutarate + CoA + NADP⁺ = succinyl-CoA + CO₂ + NADPH

Other name(s):

oxoglutarate dehydrogenase (NADP)

Systematic name:

2-oxoglutarate:NADP⁺ 2-oxidoreductase (CoA-succinylating)

Comments:

The Euglena enzyme can also use NAD⁺ as acceptor, but more slowly.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 126469-85-0

References:

1.	Inui, H., Miyatake, K., Nakano, Y. and Kitaoka, S. Occurrence of oxygen-sensitive, NADP +-dependent pyruvate dehydrogenase in mitochondria of Euglena gracilis. J. Biochem. (Tokyo) 96 (1984) 931–934. [PMID: 6438078]

[EC 1.2.1.52 created 1989]

1.2.1.53

Accepted name:

4-hydroxyphenylacetaldehyde dehydrogenase

Reaction:

4-hydroxyphenylacetaldehyde + NAD⁺ + H₂O = 4-hydroxyphenylacetate + NADH + 2 H⁺

Other name(s):

4-HPAL dehydrogenase

Systematic name:

4-hydroxyphenylacetaldehyde:NAD⁺ oxidoreductase

Comments:

With EC 4.2.1.87 octopamine dehydratase, brings about the metabolism of octopamine in Pseudomonas.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 109456-56-6

References:

1.	Cuskey, S.M., Peccoraro, V. and Olsen, R.H. Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes. J. Bacteriol. 169 (1987) 2398–2404. [DOI] [PMID: 3034855]

[EC 1.2.1.53 created 1989]

1.2.1.54

Accepted name:

γ-guanidinobutyraldehyde dehydrogenase

Reaction:

4-guanidinobutanal + NAD⁺ + H₂O = 4-guanidinobutanoate + NADH + 2 H⁺

Other name(s):

α-guanidinobutyraldehyde dehydrogenase; 4-guanidinobutyraldehyde dehydrogenase; GBAL dehydrogenase

Systematic name:

4-guanidinobutanal:NAD⁺ 1-oxidoreductase

Comments:

Involved in the degradation of arginine in Pseudomonas putida (cf. EC 1.2.1.19 aminobutyraldehyde dehydrogenase).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 56831-75-5

References:

1.	Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K. 4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida. Agric. Biol. Chem. 50 (1986) 2009–2016.

[EC 1.2.1.54 created 1989]

1.2.1.55

Transferred entry:

(R)-3-hydroxyacid ester dehydrogenase. Now EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase

[EC 1.2.1.55 created 1990, deleted 2003]

1.2.1.56

Transferred entry:

(S)-3-hydroxyacid ester dehydrogenase. Now EC 1.1.1.280, (S)-3-hydroxyacid-ester dehydrogenase

[EC 1.2.1.56 created 1990, deleted 2003]

1.2.1.57

Accepted name:

butanal dehydrogenase

Reaction:

butanal + CoA + NAD(P)⁺ = butanoyl-CoA + NAD(P)H + H⁺

Systematic name:

butanal:NAD(P)⁺ oxidoreductase (CoA-acylating)

Comments:

Also acts on acetaldehyde, but more slowly.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 116412-25-0

References:

1.	Palosaari, N.R. and Rogers, P. Purification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium acetobutylicum. J. Bacteriol. 170 (1988) 2971–2976. [DOI] [PMID: 3384801]

[EC 1.2.1.57 created 1992]

1.2.1.58

Accepted name:

phenylglyoxylate dehydrogenase (acylating)

Reaction:

phenylglyoxylate + NAD⁺ + CoA = benzoyl-S-CoA + CO₂ + NADH

Systematic name:

phenylglyoxylate:NAD⁺ oxidoreductase

Comments:

Requires thiamine diphosphate as cofactor. The enzyme from the denitrifying bacterium Azoarcus evansii is specific for phenylglyoxylate. 2-Oxoisovalerate is oxidized at 15% of the rate for phenylglyoxylate. Also reduces viologen dyes. Contains iron-sulfur centres and FAD.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 205510-78-7

References:

1.	Hirsch, W., Schägger, H. and Fuchs, G. Phenylglyoxylate:NAD⁺ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Axoarcus evansii. Eur. J. Biochem. 251 (1998) 907–915. [DOI] [PMID: 9490067]

[EC 1.2.1.58 created 1999]

1.2.1.59

Accepted name:

glyceraldehyde-3-phosphate dehydrogenase (NAD(P)⁺) (phosphorylating)

Reaction:

D-glyceraldehyde 3-phosphate + phosphate + NAD(P)⁺ = 3-phospho-D-glyceroyl phosphate + NAD(P)H + H⁺

Other name(s):

triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating)

Systematic name:

D-glyceraldehyde 3-phosphate:NAD(P)⁺ oxidoreductase (phosphorylating)

Comments:

NAD⁺ and NADP⁺ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP⁺) (phosphorylating), which are NAD⁺- and NADP⁺-dependent, respectively.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 39369-25-0

References:

1.	Valverde, F., Losada, M. and Serrano, A. Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. In: P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, pp. 959–962.
2.	Valverde, F., Losada, M. and Serrano, A. Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. J. Bacteriol. 179 (1997) 4513–4522. [DOI] [PMID: 9226260]

[EC 1.2.1.59 created 1999]

1.2.1.60

Accepted name:

5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase

Reaction:

5-carboxymethyl-2-hydroxymuconate semialdehyde + H₂O + NAD⁺ = 5-carboxymethyl-2-hydroxymuconate + NADH + 2 H⁺

Other name(s):

carboxymethylhydroxymuconic semialdehyde dehydrogenase

Systematic name:

5-carboxymethyl-2-hydroxymuconic-semialdehyde:NAD⁺ oxidoreductase

Comments:

Involved in the tyrosine degradation pathway in Arthrobacter sp.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 63241-20-3

References:

1.	Blakley, E.R. The catabolism of L-tyrosine by an Arthrobacter sp. Can. J. Microbiol. 23 (1977) 1128–1139. [PMID: 20216]
2.	Alonso, J.M. and Garrido-Pertierra, A. Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli. Biochim. Biophys. Acta 719 (1982) 165–167. [DOI] [PMID: 6756482]
3.	Cooper, R.A. and Skinner, M.A. Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli. J. Bacteriol. 143 (1980) 302–306. [PMID: 6995433]
4.	Garrido-Pertierra, A. and Cooper, R.A. Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate pathway of Escherichia coli. Eur. J. Biochem. 117 (1981) 581–584. [DOI] [PMID: 7026235]

[EC 1.2.1.60 created 2000]

1.2.1.61

Accepted name:

4-hydroxymuconic-semialdehyde dehydrogenase

Reaction:

4-hydroxymuconic semialdehyde + NAD⁺ + H₂O = maleylacetate + NADH + 2 H⁺

For diagram of 4-nitrophenol metabolism, click here

Systematic name:

4-hydroxymuconic-semialdehyde:NAD⁺ oxidoreductase

Comments:

Involved in the 4-nitrophenol degradation pathway.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc

References:

1.	Spain, J.C. and Gibson, D.T. Pathway for bioremediation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 57 (1991) 812–819. [PMID: 16348446]

[EC 1.2.1.61 created 2000]

1.2.1.62

Accepted name:

4-formylbenzenesulfonate dehydrogenase

Reaction:

4-formylbenzenesulfonate + NAD⁺ + H₂O = 4-sulfobenzoate + NADH + 2 H⁺

Systematic name:

4-formylbenzenesulfonate:NAD⁺ oxidoreductase

Comments:

Involved in the toluene-4-sulfonate degradation pathway.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 167973-68-4

References:

1.	Junker, F., Saller, E., Schläfli Oppenberg, H.R., Kroneck, P.M., Leisinger, T. and Cook, A.M. Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2. Microbiology 142 (1996) 2419–2427. [DOI] [PMID: 8828208]
2.	Junker, F., Kiewitz, R. and Cook, A.M. Characterization of the p-toluenesulfonate operon tsaMBCD and tsaR in Comamonas testosteroni T-2. J. Bacteriol. 179 (1997) 919–927. [DOI] [PMID: 9006050]

[EC 1.2.1.62 created 2000]

1.2.1.63

Accepted name:

6-oxohexanoate dehydrogenase

Reaction:

6-oxohexanoate + NADP⁺ + H₂O = adipate + NADPH + 2 H⁺

Systematic name:

6-oxohexanoate:NADP⁺ oxidoreductase

Comments:

Last step in the cyclohexanol degradation pathway in Acinetobacter sp.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 62628-29-9

References:

1.	Davey, J.F. and Trudgill, P.W. The metabolism of trans-cyclohexan-1,2-diol by an Acinetobacter species. Eur. J. Biochem. 74 (1977) 115–127. [DOI] [PMID: 856571]
2.	Donoghue, N.A. and Trudgill, P.W. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60 (1975) 1–7. [DOI] [PMID: 1261]

[EC 1.2.1.63 created 2000]

1.2.1.64

Accepted name:

4-hydroxybenzaldehyde dehydrogenase (NAD⁺)

Reaction:

4-hydroxybenzaldehyde + NAD⁺ + H₂O = 4-hydroxybenzoate + NADH + 2 H⁺

Other name(s):

p-hydroxybenzaldehyde dehydrogenase (ambiguous); 4-hydroxybenzaldehyde dehydrogenase (ambiguous)

Systematic name:

4-hydroxybenzaldehyde:NAD⁺ oxidoreductase

Comments:

The bacterial enzyme (characterized from an unidentified denitrifying bacterium) is involved in an anaerobic toluene degradation pathway. The plant enzyme is involved in formation of 4-hydroxybenzoate, a cell wall-bound phenolic acid that plays a major role in plant defense against pathogens. cf. EC 1.2.1.96, 4-hydroxybenzaldehyde dehydrogenase (NADP⁺).

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 61229-72-9

References:

1.	Bossert, I.D., Whited, G., Gibson, D.T. and Young, L.Y. Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium. J. Bacteriol. 171 (1989) 2956–2962. [DOI] [PMID: 2722739]
2.	Sircar, D. and Mitra, A. Evidence for p-hydroxybenzoate formation involving enzymatic phenylpropanoid side-chain cleavage in hairy roots of Daucus carota. J. Plant Physiol. 165 (2008) 407–414. [DOI] [PMID: 17658659]

[EC 1.2.1.64 created 2000, modified 2015]

1.2.1.65

Accepted name:

salicylaldehyde dehydrogenase

Reaction:

salicylaldehyde + NAD⁺ + H₂O = salicylate + NADH + 2 H⁺

Glossary:

salicylaldehyde = 2-hydroxybenzaldehyde

Systematic name:

salicylaldehyde:NAD⁺ oxidoreductase

Comments:

Involved in the naphthalene degradation pathway in some bacteria.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 55354-34-2

References:

1.	Eaton, R. and Chapman, P.J. Bacterial metabolism of naphthalene: construction and use of recombinant bacteria to study ring cleavage of 1,2-dihydroxynaphthalene and subsequent reactions. J. Bacteriol. 174 (1992) 7542–7554. [DOI] [PMID: 1447127]

[EC 1.2.1.65 created 2000, modified 2011]

1.2.1.66

Transferred entry:

mycothiol-dependent formaldehyde dehydrogenase. Now EC 1.1.1.306, S-(hydroxymethyl)mycothiol dehydrogenase

[EC 1.2.1.66 created 2000, deleted 2010]

1.2.1.67

Accepted name:

vanillin dehydrogenase

Reaction:

vanillin + NAD⁺ + H₂O = vanillate + NADH + 2 H⁺

Glossary:

vanillate = 4-hydroxy-3-methoxybenzoate
vanillin = 4-hydroxy-3-methoxybenzaldehyde

Systematic name:

vanillin:NAD⁺ oxidoreductase

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 189767-93-9

References:

1.	Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582–1585. [PMID: 6870241]

[EC 1.2.1.67 created 2000]

1.2.1.68

Accepted name:

coniferyl-aldehyde dehydrogenase

Reaction:

coniferyl aldehyde + H₂O + NAD(P)⁺ = ferulate + NAD(P)H + 2 H⁺

For diagram of reaction, click here

Systematic name:

coniferyl aldehyde:NAD(P)⁺ oxidoreductase

Comments:

Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 208540-41-4

References:

1.	Achterholt, S., Priefert, H. and Steinbuchel, A. Purification and characterization of the coniferyl 2-hydroxy-1,4-benzoquinonealdehyde dehydrogenase from Pseudomonas sp. Strain HR199 and molecular characterization of the gene. J. Bacteriol. 180 (1998) 4387–4391. [PMID: 9721273]

[EC 1.2.1.68 created 2000]

1.2.1.69

Accepted name:

fluoroacetaldehyde dehydrogenase

Reaction:

fluoroacetaldehyde + NAD⁺ + H₂O = fluoroacetate + NADH + 2 H⁺

Systematic name:

fluoroacetaldehyde:NAD⁺ oxidoreductase

Comments:

The enzyme from Streptomyces cattleya has a high affinity for fluoroacetate and glycolaldehyde but not for acetaldehyde.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 387336-50-7

References:

1.	Murphy, C.D., Moss, S.J. and O'Hagan, D. Isolation of an aldehyde dehydrogenase involved in the oxidation of fluoroacetaldehyde to fluoroacetate in Streptomyces cattleya. Appl. Environ. Microbiol. 67 (2001) 4919–4921. [DOI] [PMID: 11571203]
2.	Murphy, C.D., Schaffrath, C. and O'Hagan, D. Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya. Chemosphere 52 (2003) 455–461. [DOI] [PMID: 12738270]

[EC 1.2.1.69 created 2003]

1.2.1.70

Accepted name:

glutamyl-tRNA reductase

Reaction:

L-glutamate 1-semialdehyde + NADP⁺ + tRNA^Glu = L-glutamyl-tRNA^Glu + NADPH + H⁺

For diagram of the early stages of porphyrin biosynthesis, click here

Systematic name:

L-glutamate-semialdehyde:NADP⁺ oxidoreductase (L-glutamyl-tRNA^Glu-forming)

Comments:

This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway. The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 119940-26-0

References:

1.	von Wettstein, D., Gough, S. and Kannangara, C.G. Chlorophyll biosynthesis. Plant Cell 7 (1995) 1039–1057. [DOI] [PMID: 12242396]
2.	Pontoppidan, B. and Kannangara, C.G. Purification and partial characterisation of barley glutamyl-tRNA^Glu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur. J. Biochem. 225 (1994) 529–537. [DOI] [PMID: 7957167]
3.	Schauer, S., Chaturvedi, S., Randau, L., Moser, J., Kitabatake, M., Lorenz, S., Verkamp, E., Schubert, W.D., Nakayashiki, T., Murai, M., Wall, K., Thomann, H.-U., Heinz, D.W., Inokuchi, H, Söll, D. and Jahn, D. Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate. J. Biol. Chem. 277 (2002) 48657–48663. [DOI] [PMID: 12370189]

[EC 1.2.1.70 created 2004]

1.2.1.71

Accepted name:

succinylglutamate-semialdehyde dehydrogenase

Reaction:

N-succinyl-L-glutamate 5-semialdehyde + NAD⁺ + H₂O = N-succinyl-L-glutamate + NADH + 2 H⁺

For diagram of arginine catabolism, click here

Other name(s):

succinylglutamic semialdehyde dehydrogenase; N-succinylglutamate 5-semialdehyde dehydrogenase; SGSD; AruD; AstD

Systematic name:

N-succinyl-L-glutamate 5-semialdehyde:NAD⁺ oxidoreductase

Comments:

This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [3,6].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Vander Wauven, C., Jann, A., Haas, D., Leisinger, T. and Stalon, V. N²-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa. Arch. Microbiol. 150 (1988) 400–404. [PMID: 3144259]
2.	Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882–886. [PMID: 2865249]
3.	Tricot, C., Vander Wauven, C., Wattiez, R., Falmagne, P. and Stalon, V. Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine. Eur. J. Biochem. 224 (1994) 853–861. [DOI] [PMID: 7523119]
4.	Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280–7290. [DOI] [PMID: 9393691]
5.	Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278–4286. [PMID: 9696779]
6.	Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314–352. [PMID: 3534538]
7.	Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Erratum report: Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 51 (1987) 178. [PMID: 16350242]

[EC 1.2.1.71 created 2006]

1.2.1.72

Accepted name:

erythrose-4-phosphate dehydrogenase

Reaction:

D-erythrose 4-phosphate + NAD⁺ + H₂O = 4-phosphoerythronate + NADH + 2 H⁺

For diagram of pyridoxal biosynthesis, click here

Other name(s):

erythrose 4-phosphate dehydrogenase; E4PDH; GapB; Epd dehydrogenase; E4P dehydrogenase

Systematic name:

D-erythrose 4-phosphate:NAD⁺ oxidoreductase

Comments:

This enzyme was originally thought to be a glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), but this has since been disproved, as glyceraldehyde 3-phosphate is not a substrate [1,2]. Forms part of the pyridoxal-5′-phosphate cofactor biosynthesis pathway in Escherichia coli, along with EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5′-phosphate synthase) and EC 1.4.3.5 (pyridoxamine-phosphate oxidase).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 131554-04-6

References:

1.	Zhao, G., Pease, A.J., Bharani, N. and Winkler, M.E. Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5′-phosphate biosynthesis. J. Bacteriol. 177 (1995) 2804–2812. [DOI] [PMID: 7751290]
2.	Boschi-Muller, S., Azza, S., Pollastro, D., Corbier, C. and Branlant, G. Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 272 (1997) 15106–15112. [DOI] [PMID: 9182530]
3.	Yang, Y., Zhao, G., Man, T.K. and Winkler, M.E. Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5′-phosphate coenzyme biosynthesis in Escherichia coli K-12. J. Bacteriol. 180 (1998) 4294–4299. [PMID: 9696782]

[EC 1.2.1.72 created 2006]

1.2.1.73

Accepted name:

sulfoacetaldehyde dehydrogenase

Reaction:

2-sulfoacetaldehyde + H₂O + NAD⁺ = sulfoacetate + NADH + 2 H⁺

Glossary:

2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate

Other name(s):

SafD

Systematic name:

2-sulfoacetaldehyde:NAD⁺ oxidoreductase

Comments:

This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD⁺ cannot be replaced by NADP⁺. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

Krejčík, Z., Denger, K., Weinitschke, S., Hollemeyer, K., Pačes, V., Cook, A.M. and Smits, T.H.M. Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch. Microbiol. 190 (2008) 159–168. [DOI] [PMID: 18506422]

[EC 1.2.1.73 created 2008]

1.2.1.74

Accepted name:

abieta-7,13-dien-18-al dehydrogenase

Reaction:

abieta-7,13-dien-18-al + H₂O + NAD⁺ = abieta-7,13-dien-18-oate + NADH + H⁺

For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here

Glossary:

abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde
abieta-7,13-dien-18-oate = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carboxylate

Other name(s):

abietadienal dehydrogenase (ambiguous)

Systematic name:

abieta-7,13-dien-18-al:NAD⁺ oxidoreductase

Comments:

Abietic acid is the principle component of conifer resin. This enzyme catalyses the last step of the pathway of abietic acid biosynthesis in Abies grandis (grand fir). The activity has been demonstrated in cell-free stem extracts of A. grandis, was present in the cytoplasm, and required NAD⁺ as cofactor [1]. The enzyme is expressed constitutively at a high level, and is not inducible by wounding of the plant tissue [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258–266. [DOI] [PMID: 8311462]
2.	Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999–1005. [PMID: 12232380]

[EC 1.2.1.74 created 2009, modified 2012]

1.2.1.75

Accepted name:

malonyl-CoA reductase (malonate semialdehyde-forming)

Reaction:

malonate semialdehyde + CoA + NADP⁺ = malonyl-CoA + NADPH + H⁺

For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here

Other name(s):

NADP-dependent malonyl CoA reductase; malonyl CoA reductase (NADP); malonyl CoA reductase (malonate semialdehyde-forming)

Systematic name:

malonate semialdehyde:NADP⁺ oxidoreductase (malonate semialdehyde-forming)

Comments:

Requires Mg²⁺. Catalyses the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO₂ fixation pathways found in some green non-sulfur phototrophic bacteria and some thermoacidophilic archaea, respectively [1,2]. The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits [3]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the next reaction in the pathway, EC 1.1.1.298 [3-hydroxypropionate dehydrogenase (NADP⁺)] [4].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Strauss, G. and Fuchs, G. Enzymes of a novel autotrophic CO₂ fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur. J. Biochem. 215 (1993) 633–643. [DOI] [PMID: 8354269]
2.	Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
3.	Alber, B., Olinger, M., Rieder, A., Kockelkorn, D., Jobst, B., Hugler, M. and Fuchs, G. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J. Bacteriol. 188 (2006) 8551–8559. [DOI] [PMID: 17041055]
4.	Hugler, M., Menendez, C., Schagger, H. and Fuchs, G. Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO₂ fixation. J. Bacteriol. 184 (2002) 2404–2410. [DOI] [PMID: 11948153]

[EC 1.2.1.75 created 2009]

1.2.1.76

Accepted name:

succinate-semialdehyde dehydrogenase (acylating)

Reaction:

succinate semialdehyde + CoA + NADP⁺ = succinyl-CoA + NADPH + H⁺

For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here

Other name(s):

succinyl-coA reductase; coenzyme-A-dependent succinate-semialdehyde dehydrogenase

Systematic name:

succinate semialdehyde:NADP⁺ oxidoreductase (CoA-acylating)

Comments:

Catalyses the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde. The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation [1], and in Metallosphaera sedula, where it participates in the 3-hydroxypropanonate/4-hydroxybutanoate cycle, an autotrophic CO₂ fixation pathway found in some thermoacidophilic archaea [2,3].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Sohling, B. and Gottschalk, G. Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 212 (1993) 121–127. [DOI] [PMID: 8444151]
2.	Alber, B., Olinger, M., Rieder, A., Kockelkorn, D., Jobst, B., Hugler, M. and Fuchs, G. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J. Bacteriol. 188 (2006) 8551–8559. [DOI] [PMID: 17041055]
3.	Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]

[EC 1.2.1.76 created 2009]

1.2.1.77

Accepted name:

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP⁺)

Reaction:

3,4-didehydroadipyl-CoA semialdehyde + NADP⁺ + H₂O = 3,4-didehydroadipyl-CoA + NADPH + H⁺

For diagram of Benzoyl-CoA catabolism, click here

Other name(s):

BoxD; 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase

Systematic name:

3,4-didehydroadipyl-CoA semialdehyde:NADP⁺ oxidoreductase

Comments:

This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc

References:

1.	Gescher, J., Ismail, W., Olgeschlager, E., Eisenreich, W., Worth, J. and Fuchs, G. Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in Azoarcus evansii: conversion of ring cleavage product by 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase. J. Bacteriol. 188 (2006) 2919–2927. [DOI] [PMID: 16585753]
2.	Bains, J. and Boulanger, M.J. Structural and biochemical characterization of a novel aldehyde dehydrogenase encoded by the benzoate oxidation pathway in Burkholderia xenovorans LB400. J. Mol. Biol. 379 (2008) 597–608. [DOI] [PMID: 18462753]

[EC 1.2.1.77 created 2010]

1.2.1.78

Accepted name:

2-formylbenzoate dehydrogenase

Reaction:

2-formylbenzoate + NAD⁺ + H₂O = o-phthalic acid + NADH + H⁺

Glossary:

o-phthalic acid = benzene-1,2-dicarboxylic acid
2-formylbenzoate = 2-carboxybenzaldehyde

Other name(s):

2-carboxybenzaldehyde dehydrogenase; 2CBAL dehydrogenase; PhdK

Systematic name:

2-formylbenzoate:NAD⁺ oxidoreductase

Comments:

The enzyme is involved in phenanthrene degradation.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Iwabuchi, T. and Harayama, S. Biochemical and genetic characterization of 2-carboxybenzaldehyde dehydrogenase, an enzyme involved in phenanthrene degradation by Nocardioides sp. strain KP7. J. Bacteriol. 179 (1997) 6488–6494. [DOI] [PMID: 9335300]
2.	Kiyohara, H., Nagao, K. and Yano, K. Isolation and some properties of NAD-linked 2-carboxybenzaldehyde dehydrogenase in Alcaligenes faecalis AFK 2 grown on phenanthrene. J. Gen. Appl. Microbiol. 27 (1981) 443–455.

[EC 1.2.1.78 created 2010]

1.2.1.79

Accepted name:

succinate-semialdehyde dehydrogenase (NADP⁺)

Reaction:

succinate semialdehyde + NADP⁺ + H₂O = succinate + NADPH + 2 H⁺

For diagram of the citric acid cycle, click here

Other name(s):

succinic semialdehyde dehydrogenase (NADP⁺); succinyl semialdehyde dehydrogenase (NADP⁺); succinate semialdehyde:NADP⁺ oxidoreductase; NADP-dependent succinate-semialdehyde dehydrogenase; GabD

Systematic name:

succinate-semialdehyde:NADP⁺ oxidoreductase

Comments:

This enzyme participates in the degradation of glutamate and 4-aminobutyrate. It is similar to EC 1.2.1.24 [succinate-semialdehyde dehydrogenase (NAD⁺)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)⁺)], but is specific for NADP⁺. The enzyme from Escherichia coli is 20-fold more active with NADP⁺ than NAD⁺ [2].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Bartsch, K., von Johnn-Marteville, A. and Schulz, A. Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD). J. Bacteriol. 172 (1990) 7035–7042. [DOI] [PMID: 2254272]
2.	Jaeger, M., Rothacker, B. and Ilg, T. Saturation transfer difference NMR studies on substrates and inhibitors of succinic semialdehyde dehydrogenases. Biochem. Biophys. Res. Commun. 372 (2008) 400–406. [DOI] [PMID: 18474219]

[EC 1.2.1.79 created 2010]

1.2.1.80

Accepted name:

long-chain acyl-[acyl-carrier-protein] reductase

Reaction:

a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)⁺ = a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H⁺

Glossary:

a long-chain aldehyde = an aldehyde derived from a fatty acid with an aliphatic chain of 13-22 carbons.
an [acyl-carrier protein] = ACP = [acp]

Other name(s):

long-chain acyl-[acp] reductase; fatty acyl-[acyl-carrier-protein] reductase; acyl-[acp] reductase

Systematic name:

long-chain-aldehyde:NAD(P)⁺ oxidoreductase (acyl-[acyl-carrier protein]-forming)

Comments:

Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C₁₆ and C₁₈ activated fatty acids. Requires Mg²⁺.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Schirmer, A., Rude, M.A., Li, X., Popova, E. and del Cardayre, S.B. Microbial biosynthesis of alkanes. Science 329 (2010) 559–562. [DOI] [PMID: 20671186]

[EC 1.2.1.80 created 2011]

1.2.1.81

Accepted name:

sulfoacetaldehyde dehydrogenase (acylating)

Reaction:

2-sulfoacetaldehyde + CoA + NADP⁺ = sulfoacetyl-CoA + NADPH + H⁺

Glossary:

2-sulfoacetaldehyde = 2-oxoethanesulfonate

Other name(s):

SauS

Systematic name:

2-sulfoacetaldehyde:NADP⁺ oxidoreductase (CoA-acetylating)

Comments:

The enzyme is involved in degradation of sulfoacetate. In this pathway the reaction is catalysed in the reverse direction. The enzyme is specific for sulfoacetaldehyde and NADP⁺.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

1.	Weinitschke, S., Hollemeyer, K., Kusian, B., Bowien, B., Smits, T.H. and Cook, A.M. Sulfoacetate is degraded via a novel pathway involving sulfoacetyl-CoA and sulfoacetaldehyde in Cupriavidus necator H16. J. Biol. Chem. 285 (2010) 35249–35254. [DOI] [PMID: 20693281]

[EC 1.2.1.81 created 2011]