ExplorEnz: EC 1.14.99.4*

Your query returned 11 entries. Printable version

1.14.99.4

Accepted name:

progesterone monooxygenase

Reaction:

progesterone + reduced acceptor + O₂ = testosterone acetate + acceptor + H₂O

Other name(s):

progesterone hydroxylase

Systematic name:

progesterone,hydrogen-donor:oxygen oxidoreductase (hydroxylating)

Comments:

Has a wide specificity. A single enzyme from ascomycete the Neonectria radicicola (EC 1.14.13.54 ketosteroid monooxygenase) catalyses both this reaction and that catalysed by EC 1.14.99.12 androst-4-ene-3,17-dione monooxygenase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-85-2

References:

1.	Rahim, M.A. and Sih, C.J. Mechanisms of steroid oxidation by microorganisms. XI. Enzymatic cleavage of the pregnane side chain. J. Biol. Chem. 241 (1966) 3615–3623. [PMID: 5950688]

[EC 1.14.99.4 created 1972, modified 1999]

1.14.99.40

Transferred entry:

5,6-dimethylbenzimidazole synthase. Now EC 1.13.11.79, 5,6-dimethylbenzimidazole synthase

[EC 1.14.99.40 created 2010, deleted 2014]

1.14.99.41

Transferred entry:

all-trans-8′-apo-β-carotenal 15,15′-oxygenase. Now EC 1.13.11.75, all-trans-8′-apo-β-carotenal 15,15′-oxygenase

[EC 1.14.99.41 created 2010, deleted 2013]

1.14.99.42

Transferred entry:

zeaxanthin 7,8-dioxygenase. Now EC 1.13.11.84, crocetin dialdehyde synthase

[EC 1.14.99.42 created 2011, modified 2014, deleted 2017]

1.14.99.43

Transferred entry:

β-amyrin 24-hydroxylase. Now EC 1.14.14.134, β-amyrin 24-hydroxylase

[EC 1.14.99.43 created 2011, deleted 2018]

1.14.99.44

Accepted name:

diapolycopene oxygenase

Reaction:

4,4′-diapolycopene + 4 reduced acceptor + 4 O₂ = 4,4′-diapolycopenedial + 4 acceptor + 6 H₂O

For diagram of C₃₀ carotenoid biosynthesis, click here

Other name(s):

crtP (ambiguous)

Systematic name:

4,4′-diapolycopene,AH₂:oxygen oxidoreductase (4,4′-hydroxylating)

Comments:

Little activity with neurosporene or lycopene. Involved in the biosynthesis of C₃₀ carotenoids such as staphyloxanthin. The enzyme oxidizes each methyl group to the hydroxymethyl and then a dihydroxymethyl group, followed by the spontaneous loss of water to give an aldehyde group.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Mijts, B.N., Lee, P.C. and Schmidt-Dannert, C. Identification of a carotenoid oxygenase synthesizing acyclic xanthophylls: combinatorial biosynthesis and directed evolution. Chem. Biol. 12 (2005) 453–460. [DOI] [PMID: 15850982]
2.	Tao, L., Schenzle, A., Odom, J.M. and Cheng, Q. Novel carotenoid oxidase involved in biosynthesis of 4,4′-diapolycopene dialdehyde. Appl. Environ. Microbiol. 71 (2005) 3294–3301. [DOI] [PMID: 15933032]

[EC 1.14.99.44 created 2011]

1.14.99.45

Transferred entry:

carotene ε-monooxygenase. Now EC 1.14.14.158, carotene ε-monooxygenase

[EC 1.14.99.45 created 2011, deleted 2018]

1.14.99.46

Accepted name:

pyrimidine oxygenase

Reaction:

(1) uracil + FMNH₂ + O₂ + NADH = (Z)-3-ureidoacrylate + H₂O + FMN + NAD⁺ + H⁺ (overall reaction)
(1a) FMNH₂ + O₂ = FMN-N⁵-peroxide
(1b) uracil + FMN-N⁵-peroxide = (Z)-3-ureidoacrylate + FMN-N⁵-oxide
(1c) FMN-N⁵-oxide + NADH = FMN + H₂O + NAD⁺ + H⁺ (spontaneous)
(2) thymine + FMNH₂ + O₂ + NADH = (Z)-2-methylureidoacrylate + H₂O + FMN + NAD⁺ + H⁺ (overall reaction)
(2a) FMNH₂ + O₂ = FMN-N⁵-peroxide
(2b) thymine + FMN-N⁵-peroxide = (Z)-2-methylureidoacrylate + FMN-N⁵-oxide
(2c) FMN-N⁵-oxide + NADH = FMN + H₂O + NAD⁺ + H⁺ (spontaneous)

Glossary:

(Z)-3-ureidoacrylate = (2Z)-3-(carbamoylamino)prop-2-enoate
(Z)-2-methylureidoacrylate = (2Z)-3-(carbamoylamino)-2-methylprop-2-enoate

Other name(s):

rutA (gene name)

Systematic name:

uracil,FMNH₂:oxygen oxidoreductase (uracil hydroxylating, ring-opening)

Comments:

The enzyme participates in the Rut pyrimidine catabolic pathway. The flavin-N⁵-oxide that is formed by the enzyme reacts spontaneously with NADH to give oxidized flavin, releasing a water molecule.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Mukherjee, T., Zhang, Y., Abdelwahed, S., Ealick, S.E. and Begley, T.P. Catalysis of a flavoenzyme-mediated amide hydrolysis. J. Am. Chem. Soc. 132 (2010) 5550–5551. [DOI] [PMID: 20369853]
2.	Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089–4102. [DOI] [PMID: 20400551]
3.	Adak, S. and Begley, T.P. RutA-catalyzed oxidative cleavage of the uracil amide involves formation of a flavin-N⁵-oxide. Biochemistry 56 (2017) 3708–3709. [PMID: 28661684]
4.	Adak, S. and Begley, T.P. Flavin-N⁵-oxide: A new, catalytic motif in flavoenzymology. Arch. Biochem. Biophys. 632 (2017) 4–10. [PMID: 28784589]
5.	Matthews, A., Saleem-Batcha, R., Sanders, J.N., Stull, F., Houk, K.N. and Teufel, R. Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases. Nat. Chem. Biol. 16 (2020) 556–563. [DOI] [PMID: 32066967]

[EC 1.14.99.46 created 2012, modified 2019]

1.14.99.47

Accepted name:

(+)-larreatricin hydroxylase

Reaction:

(+)-larreatricin + reduced acceptor + O₂ = (+)-3′-hydroxylarreatricin + acceptor + H₂O

Glossary:

(+)-larreatricin = 4,4′-[(2R,3R,4S,5R)-3,4-dimethyltetrahydrofuran-2,5-diyl]bisphenol

Systematic name:

(+)-larreatricin:oxygen 3′-hydroxylase

Comments:

Isolated from the plant Larrea tridentata (creosote bush). The enzyme has a strong preference for the 3′ position of (+)-larreatricin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Cho, M.H., Moinuddin, S.G., Helms, G.L., Hishiyama, S., Eichinger, D., Davin, L.B. and Lewis, N.G. (+)-Larreatricin hydroxylase, an enantio-specific polyphenol oxidase from the creosote bush (Larrea tridentata). Proc. Natl. Acad. Sci. USA 100 (2003) 10641–10646. [DOI] [PMID: 12960376]

[EC 1.14.99.47 created 2012]

1.14.99.48

Accepted name:

heme oxygenase (staphylobilin-producing)

Reaction:

(1) protoheme + 5 reduced acceptor + 4 O₂ = β-staphylobilin + Fe²⁺ + formaldehyde + 5 acceptor + 4 H₂O
(2) protoheme + 5 reduced acceptor + 4 O₂ = δ-staphylobilin + Fe²⁺ + formaldehyde + 5 acceptor + 4 H₂O

For diagram of staphylobilin biosynthesis, click here

Glossary:

β-staphylobilin = 10-oxo-β-bilirubin = 3,7-bis(2-carboxyethyl)-2,8,13,18-tetramethyl-12,17-divinylbiladiene-ac-1,10,19(21H,24H)-trione
δ-staphylobilin = 10-oxo-δ-bilirubin = 3,7-bis(2-carboxyethyl)-2,8,12,17-tetramethyl-13,18-divinylbiladiene-ac-1,10,19(21H,24H)-trione

Other name(s):

haem oxygenase (ambiguous); heme oxygenase (decyclizing) (ambiguous); heme oxidase (ambiguous); haem oxidase (ambiguous); heme oxygenase (ambiguous); isdG (gene name); isdI (gene name)

Systematic name:

protoheme,hydrogen-donor:oxygen oxidoreductase (δ/β-methene-oxidizing, hydroxylating)

Comments:

This enzyme, which is found in some pathogenic bacteria, is involved in an iron acquisition system that catabolizes the host’s hemoglobin. The two enzymes from the bacterium Staphylococcus aureus, encoded by the isdG and isdI genes, produce 67.5 % and 56.2 % δ-staphylobilin, respectively.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Reniere, M.L., Ukpabi, G.N., Harry, S.R., Stec, D.F., Krull, R., Wright, D.W., Bachmann, B.O., Murphy, M.E. and Skaar, E.P. The IsdG-family of haem oxygenases degrades haem to a novel chromophore. Mol. Microbiol. 75 (2010) 1529–1538. [DOI] [PMID: 20180905]
2.	Matsui, T., Nambu, S., Ono, Y., Goulding, C.W., Tsumoto, K. and Ikeda-Saito, M. Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide. Biochemistry 52 (2013) 3025–3027. [DOI] [PMID: 23600533]
3.	Streit, B.R., Kant, R., Tokmina-Lukaszewska, M., Celis, A.I., Machovina, M.M., Skaar, E.P., Bothner, B. and DuBois, J.L. Time-resolved studies of IsdG protein identify molecular signposts along the non-canonical heme oxygenase pathway. J. Biol. Chem. 291 (2016) 862–871. [DOI] [PMID: 26534961]

[EC 1.14.99.48 created 2013]

1.14.99.49

Transferred entry:

2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase. Now EC 1.14.15.31, 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase

[EC 1.14.99.49 created 2014, deleted 2018]