2,5-diketocamphane 1,2-monooxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.14.108 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108, 2,5-diketocamphane lactonizing enzyme, ketolactonase I, 2,5-diketocamphane 1,2-monooxygenase oxygenating component, 2,5-DKCMO, camphor 1,2-monooxygenase, camphor ketolactonase I) is an enzyme with systematic name (+)-bornane-2,5-dione,NADH:oxygen oxidoreductase (1,2-lactonizing). [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction
2,5-diketocamphane 1,2-monooxygenase is a flavoprotein (FMN) which requires Fe2+.
Rubredoxins are a class of low-molecular-weight iron-containing proteins found in sulfur-metabolizing bacteria and archaea. Sometimes rubredoxins are classified as iron-sulfur proteins; however, in contrast to iron-sulfur proteins, rubredoxins do not contain inorganic sulfide. Like cytochromes, ferredoxins and Rieske proteins, rubredoxins are thought to participate in electron transfer in biological systems. Recent work in bacteria and algae have led to the hypothesis that some rubredoxins may instead have a role in delivering iron to metalloproteins.
Muconate lactonizing enzymes are involved in the breakdown of lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates as a part of the β-ketoadipate pathway in soil microbes. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes. MLEs consist of several strands which have variable reaction favorable parts therefore the configuration of the strands affect its ability to accept protons. The bacterial MLEs belong to the enolase superfamily, several structures from which are known. MLEs have an identifying structure made up of two proteins and two Magnesium ions as well as various classes depending on whether it is bacterial or eukaryotic. The reaction mechanism that MLEs undergo are the reverse of beta-elimination in which the enolate alpha-carbon is protonated. MLEs can undergo mutations caused by a deletion of catB structural genes which can cause some bacteria to lose its functions such as the ability to grow. Additional mutations to MLEs can cause its structure and function to alter and could cause the conformation to change therefore making it an inactive enzyme that is unable to bind its substrate. There is another enzyme called Mandelate Racemase that is very similar to MLEs in the structural way as well as them both being a part of the enolase superfamily. They both have the same end product even though they undergo different chemical reactions in order to reach the end product.
In enzymology, a cyclopentanol dehydrogenase (EC 1.1.1.163) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-hydroxycyclohexanone 2-monooxygenase (EC 1.14.13.66) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-hydroxyquinoline 8-monooxygenase (EC 1.14.13.61) is an enzyme that catalyzes the chemical reaction
4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.14.9) is an enzyme that catalyzes the chemical reaction
In enzymology, a camphor 1,2-monooxygenase (EC 1.14.15.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a camphor 5-monooxygenase (EC 1.14.15.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a cyclopentanone monooxygenase (EC 1.14.13.16) is an enzyme that catalyzes the chemical reaction
In enzymology, a naphthalene 1,2-dioxygenase (EC 1.14.12.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-carboxy-cis,cis-muconate cycloisomerase is an enzyme that catalyzes the chemical reaction
5-exo-hydroxycamphor dehydrogenase (EC 1.1.1.327, F-dehydrogenase, FdeH) is an enzyme with systematic name 5-exo-hydroxycamphor:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
6-Hydroxynicotinate 3-monooxygenase (EC 1.14.13.114, NicC, 6HNA monooxygenase, HNA-3-monooxygenase) is an enzyme with systematic name 6-hydroxynicotinate,NADH:oxygen oxidoreductase (3-hydroxylating, decarboxylating). This enzyme catalyses the following chemical reaction
Phenylacetyl-CoA 1,2-epoxidase (EC 1.14.13.149, ring 1,2-phenylacetyl-CoA epoxidase, phenylacetyl-CoA monooxygenase, PaaAC, PaaABC(D)E) is an enzyme with systematic name phenylacetyl-CoA:oxygen oxidoreductase (1,2-epoxidizing). This enzyme catalyses the following chemical reaction
(2,2,3-Trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase (EC 1.14.13.160, 2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase, 2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase, OTEMO) is an enzyme with systematic name ((1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA,NADPH:oxygen oxidoreductase (1,5-lactonizing). This enzyme catalyses the following chemical reaction
6-hydroxy-3-succinoylpyridine 3-monooxygenase (EC 1.14.13.163, 6-hydroxy-3-succinoylpyridine hydroxylase, hspA (gene), hspB (gene)) is an enzyme with systematic name 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate,NADH:oxygen oxidoreductase (3-hydroxylating, succinate semialdehyde releasing). This enzyme catalyses the following chemical reaction
Putidaredoxin—NAD+ reductase (EC 1.18.1.5, putidaredoxin reductase, camA (gene)) is an enzyme with systematic name putidaredoxin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
6-oxocamphor hydrolase (EC 3.7.1.18, OCH, camK (gene)) is an enzyme with systematic name bornane-2,6-dione hydrolase. This enzyme catalyses the following chemical reaction
(2,2,3-Trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase is an enzyme with systematic name ( -2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetate:CoA ligase (AMP-forming). This enzyme catalyses the following chemical reaction
4-Methylcatechol is a chemical compound. It is a component of castoreum, the exudate from the castor sacs of the mature beaver.