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1.2.1.82

Accepted name:

β-apo-4′-carotenal dehydrogenase

Reaction:

4′-apo-β,ψ-caroten-4′-al + NAD⁺ + H₂O = neurosporaxanthin + NADH + 2 H⁺

For diagram of reaction, click here

Glossary:

neurosporaxanthin = 4′-apo-β,ψ-caroten-4′-oic acid

Other name(s):

β-apo-4′-carotenal oxygenase; YLO-1; carD (gene name)

Systematic name:

4′-apo-β,ψ-carotenal:NAD⁺ oxidoreductase

Comments:

Neurosporaxanthin is responsible for the orange color of of Neurospora.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Estrada, A.F., Youssar, L., Scherzinger, D., Al-Babili, S. and Avalos, J. The ylo-1 gene encodes an aldehyde dehydrogenase responsible for the last reaction in the Neurospora carotenoid pathway. Mol. Microbiol. 69 (2008) 1207–1220. [DOI] [PMID: 18627463]
2.	Diaz-Sanchez, V., Estrada, A.F., Trautmann, D., Al-Babili, S. and Avalos, J. The gene carD encodes the aldehyde dehydrogenase responsible for neurosporaxanthin biosynthesis in Fusarium fujikuroi. FEBS J. 278 (2011) 3164–3176. [DOI] [PMID: 21749649]

[EC 1.2.1.82 created 2011, modified 2023]

1.3.99.30

Accepted name:

phytoene desaturase (3,4-didehydrolycopene-forming)

Reaction:

15-cis-phytoene + 5 acceptor = all-trans-3,4-didehydrolycopene + 5 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor = all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor = all-trans-ζ-carotene + reduced acceptor
(1c) all-trans-ζ-carotene + acceptor = all-trans-neurosporene + reduced acceptor
(1d) all-trans-neurosporene + acceptor = all-trans-lycopene + reduced acceptor
(1e) all-trans-lycopene + acceptor = all-trans-3,4-didehydrolycopene + reduced acceptor

For diagram of carotenoid biosynthesis, click here

Other name(s):

5-step phytoene desaturase; five-step phytoene desaturase; phytoene desaturase (ambiguous); Al-1

Systematic name:

15-cis-phytoene:acceptor oxidoreductase (3,4-didehydrolycopene-forming)

Comments:

This enzyme is involved in carotenoid biosynthesis and catalyses up to five desaturation steps (cf. EC 1.3.99.28 [phytoene desaturase (neurosporene-forming)], EC 1.3.99.29 [phytoene desaturase (ζ-carotene-forming)] and EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Hausmann, A. and Sandmann, G. A single five-step desaturase is involved in the carotenoid biosynthesis pathway to β-carotene and torulene in Neurospora crassa. Fungal Genet. Biol. 30 (2000) 147–153. [DOI] [PMID: 11017770]
2.	Estrada, A.F., Maier, D., Scherzinger, D., Avalos, J. and Al-Babili, S. Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new biosynthetic reaction sequence leading to neurosporaxanthin formation. Fungal Genet. Biol. 45 (2008) 1497–1505. [DOI] [PMID: 18812228]

[EC 1.3.99.30 created 2011]

1.13.11.59

Accepted name:

torulene dioxygenase

Reaction:

torulene + O₂ = 4′-apo-β,ψ-caroten-4′-al + 3-methylbut-2-enal

Glossary:

torulene = 3′,4′-didehydro-β,ψ-carotene

Other name(s):

CAO-2; CarT

Systematic name:

torulene:oxygen oxidoreductase

Comments:

It is assumed that 3-methylbut-2-enal is formed. The enzyme cannot cleave the saturated 3′,4′-bond of γ-carotene which implies that a 3′,4′-double bond is neccessary for this reaction.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Prado-Cabrero, A., Estrada, A.F., Al-Babili, S. and Avalos, J. Identification and biochemical characterization of a novel carotenoid oxygenase: elucidation of the cleavage step in the Fusarium carotenoid pathway. Mol. Microbiol. 64 (2007) 448–460. [DOI] [PMID: 17493127]
2.	Saelices, L., Youssar, L., Holdermann, I., Al-Babili, S. and Avalos, J. Identification of the gene responsible for torulene cleavage in the Neurospora carotenoid pathway. Mol. Genet. Genomics 278 (2007) 527–537. [DOI] [PMID: 17610084]
3.	Estrada, A.F., Maier, D., Scherzinger, D., Avalos, J. and Al-Babili, S. Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new biosynthetic reaction sequence leading to neurosporaxanthin formation. Fungal Genet. Biol. 45 (2008) 1497–1505. [DOI] [PMID: 18812228]

[EC 1.13.11.59 created 2011]