forming] EC 1.1.1.6: glycerol dehydrogenase EC 1.1.1.7: propanediol-phosphate dehydrogenase EC 1.1.1.8: glycerol-3-phosphate dehydrogenase (NAD+) EC 1.1.1.9:...
189 KB (24,607 words) - 12:36, 11 June 2024
Adenylyl-sulfate reductase (redirect from EC 1.8.99.2)
Adenylyl-sulfate reductase (EC 1.8.99.2) is an enzyme that catalyzes the chemical reaction of the reduction of adenylyl-sulfate/adenosine-5'-phosphosulfate...
12 KB (1,533 words) - 12:59, 26 August 2023
the reduction. The enzyme dissimilatory (bi)sulfite reductase, dsrAB (EC 1.8.99.5), that catalyzes the last step of dissimilatory sulfate reduction, is...
20 KB (2,113 words) - 01:25, 1 November 2023
List of enzymes (redirect from List of EC numbers)
Category:EC 1.6.7 now Category:EC 1.18.1 Category:EC 1.6.8 now Category:EC 1.5.1 Category:EC 1.6.99 (with other acceptors) Category:EC 1.7.1 (with NAD+...
33 KB (3,650 words) - 10:58, 5 May 2024
Hydrogensulfite reductase (redirect from EC 1.8.99.3)
In enzymology, a hydrogensulfite reductase (EC 1.8.99.3) is an enzyme that catalyzes the chemical reaction trithionate + acceptor + 2 H2O + OH- ⇌ {\displaystyle...
2 KB (210 words) - 14:29, 26 August 2023
Dissimilatory sulfite reductase (category EC 1.8.99)
Dissimilatory sulfite reductase (EC 1.8.99.5) is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction. The enzyme is essential...
4 KB (512 words) - 23:53, 6 April 2024
Ferrochelatase (redirect from EC 4.99.1.1)
Protoporphyrin ferrochelatase (EC 4.98.1.1, formerly EC 4.99.1.1, or ferrochelatase; systematic name protoheme ferro-lyase (protoporphyrin-forming)) is...
19 KB (2,000 words) - 10:52, 11 December 2023
Sulfite reductase (redirect from EC 1.8.99.1)
Sulfite reductases (EC 1.8.99.1) are enzymes that participate in sulfur metabolism. They catalyze the reduction of sulfite to hydrogen sulfide and water...
6 KB (603 words) - 13:01, 22 April 2024
Atrazine chlorohydrolase (redirect from EC 3.8.1.8)
Atrazine Chlorohydrolase (AtzA) is an enzyme (E.C.3.8.1.8), which catalyzes the conversion of atrazine to hydroxyatrazine. Bacterial degradation determines...
5 KB (535 words) - 23:51, 12 October 2023
Methylenetetrahydrofolate reductase (redirect from EC 1.7.99.5)
systematic review and meta-analysis". International Journal of Cardiology. 217: 99–108. doi:10.1016/j.ijcard.2016.04.181. PMID 27179899. Rai V, Yadav U, Kumar...
34 KB (3,737 words) - 07:12, 15 April 2024
Alcohol dehydrogenase (acceptor) (redirect from EC 1.1.99.8)
In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary alcohol + acceptor ⇌ {\displaystyle...
4 KB (346 words) - 23:50, 21 June 2024
racemase EC 5.1.1.6: threonine racemase EC 5.1.1.7: diaminopimelate epimerase EC 5.1.1.8: 4-hydroxyproline epimerase EC 5.1.1.9: arginine racemase EC 5.1.1.10:...
28 KB (3,266 words) - 15:15, 26 March 2024
Isovaleryl-CoA dehydrogenase (redirect from EC 1.3.99.10)
In enzymology, an isovaleryl-CoA dehydrogenase (EC 1.3.8.4) is an enzyme that catalyzes the chemical reaction 3-methylbutanoyl-CoA + acceptor ⇌ {\displaystyle...
3 KB (684 words) - 14:37, 26 August 2023
Iodothyronine deiodinase (redirect from EC 1.21.99.4)
Iodothyronine deiodinases (EC 1.21.99.4 and EC 1.21.99.3) are a subfamily of deiodinase enzymes important in the activation and deactivation of thyroid...
25 KB (2,460 words) - 08:18, 10 June 2024
Bile-acid 7alpha-dehydroxylase (redirect from EC 1.17.99.5)
catalyzing a total of 8 reactions. The enzymes are EC 6.2.1.7, EC 1.1.1.395, EC 1.3.1.115, EC 2.8.3.25, EC 4.2.1.106, EC 1.3.1.114, and EC 1.1.1.52. White BA,...
2 KB (263 words) - 13:21, 26 August 2023
DNA gyrase (redirect from EC 5.99.1.3)
Engle EC, Manes SH, Drlica K (January 1982). "Differential effects of antibiotics inhibiting gyrase". Journal of Bacteriology. 149 (1): 92–8. doi:10...
15 KB (1,871 words) - 05:54, 24 August 2023
NADH dehydrogenase (redirect from EC 1.6.99.3)
the acceptor. The EC term NADH dehydrogenase (ubiquinone) (EC 7.1.1.2) is defined for those with ubiquinone as the acceptor. EC 1.6.99.3 Adachi K, Okuyama...
4 KB (315 words) - 18:42, 20 October 2023
Nitrous-oxide reductase (redirect from EC 1.7.99.6)
function similar to that in the well-known aa3-type cytochrome c oxidases (EC 1.9.3.1) where it serves to receive an electron from soluble cytochromes c. Acetylene...
8 KB (891 words) - 15:48, 18 December 2023
Squalene monooxygenase (redirect from EC 1.14.99.7)
chromosome 8q24.1, is upregulated in 8q+ breast cancer and indicates poor clinical outcome in stage I and II disease". British Journal of Cancer. 99 (5): 774–80...
10 KB (1,146 words) - 01:30, 22 December 2023
Hydrazine oxidoreductase (redirect from EC 1.7.99.8)
Hydrazine oxidoreductase (EC 1.7.99.8, HAO (ambiguous)) is an enzyme with systematic name hydrazine:acceptor oxidoreductase. This enzyme catalyses the...
2 KB (140 words) - 03:24, 19 February 2024
Short-chain acyl-CoA dehydrogenase (redirect from EC 1.3.99.2)
Short-chain acyl-CoA dehydrogenase (EC 1.3.8.1, butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase...
4 KB (431 words) - 03:14, 30 March 2024
2-furoyl-CoA dehydrogenase (redirect from EC 1.3.99.8)
In enzymology, a 2-furoyl-CoA dehydrogenase (EC 1.3.99.8) is an enzyme that catalyzes the chemical reaction 2-furoyl-CoA + H2O + acceptor ⇌ {\displaystyle...
2 KB (165 words) - 12:27, 26 August 2023
Ferredoxin hydrogenase (redirect from EC 1.18.99.1)
In enzymology, ferredoxin hydrogenase (EC 1.12.7.2), also referred to as [Fe-Fe] hydrogenase, H2 oxidizing hydrogenase, H2 producing hydrogenase, bidirectional...
9 KB (1,057 words) - 23:55, 22 November 2023
Dihydrolipoamide dehydrogenase (redirect from EC 1.8.1.4)
potently stimulated by zinc". FEBS Letters. 448 (1): 190–2. Bibcode:1999FEBSL.448..190O. doi:10.1016/s0014-5793(99)00363-4. PMID 10217438. S2CID 34370150. Xia...
21 KB (2,346 words) - 00:15, 8 June 2024
EC 4.1.1.7: benzoylformate decarboxylase EC 4.1.1.8: oxalyl-CoA decarboxylase EC 4.1.1.9: malonyl-CoA decarboxylase EC 4.1.1.10: Now included with EC...
62 KB (7,931 words) - 19:04, 4 January 2024
Inositol oxygenase (redirect from EC 1.13.99.1)
D-glucuronate reductase". The Journal of Biological Chemistry. 256 (16): 8510–8. doi:10.1016/S0021-9258(19)68873-3. PMID 7263666. Charalampous FC (February...
15 KB (1,818 words) - 07:54, 9 April 2024
Sulfite oxidase (redirect from EC 1.8.3.1)
Sulfite oxidase (EC 1.8.3.1) is an enzyme in the mitochondria of all eukaryotes, with exception of the yeasts.[citation needed] It oxidizes sulfite to...
13 KB (1,683 words) - 17:02, 1 March 2024
Cholesterol 25-hydroxylase (redirect from EC 1.14.99.38)
In enzymology, a cholesterol 25-hydroxylase (EC 1.14.99.38) is an enzyme that catalyzes the chemical reaction cholesterol + AH2 + O2 ⇌ {\displaystyle \rightleftharpoons...
5 KB (569 words) - 06:50, 10 February 2024
In enzymology, an alkan-1-ol dehydrogenase (acceptor) (EC 1.1.99.20) is an enzyme that catalyzes the chemical reaction primary alcohol + acceptor ⇌ {\displaystyle...
2 KB (183 words) - 13:03, 26 August 2023
Acyl-CoA dehydrogenase (redirect from EC 1.3.99.3)
accommodate a much larger steroid-CoA substrate. ACADs are classified as EC 1.3.99.3. The medium chain acyl-CoA dehydrogenase (MCAD) is the best known structure...
17 KB (2,171 words) - 13:51, 14 July 2024