Methanogen homoaconitase | |||||||||
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Identifiers | |||||||||
EC no. | 4.2.1.114 | ||||||||
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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Methanogen homoaconitase (EC 4.2.1.114, methanogen HACN) is an enzyme with systematic name (R)-2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate-forming). [1] This enzyme catalyses the following chemical reaction
This enzyme catalyses several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea.
In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction
The enzyme methylisocitrate lyase catalyzes the chemical reaction
The enzyme 2-methylcitrate dehydratase (EC 4.2.1.79) catalyzes the chemical reaction
The enzyme 2-methylisocitrate dehydratase (EC 4.2.1.99) catalyzes the chemical reaction
The enzyme 4-oxalmesaconate hydratase (EC 4.2.1.83) catalyzes the chemical reaction
The enzyme homoaconitate hydratase (EC 4.2.1.36) catalyzes the chemical reaction
In enzymology, a 2-methylcitrate synthase (EC 2.3.3.5) is an enzyme that catalyzes the chemical reaction
Decylcitrate synthase (EC 2.3.3.2) is an enzyme that catalyzes the chemical reaction in enzymology.
In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction
Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.
Limonene-1,2-diol dehydrogenase (EC 1.1.1.297, NAD+-dependent limonene-1,2-diol dehydrogenase) is an enzyme with systematic name menth-8-ene-1,2-diol:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
Gallate dioxygenase (EC 1.13.11.57, GalA) is an enzyme with systematic name gallate:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction
Ent-kaurene oxidase (EC 1.14.14.86, Formerly EC 1.14.13.78) is an enzyme with systematic name ent-kaur-16-ene,NADPH:oxygen oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction
Epi-isozizaene 5-monooxygenase (EC 1.14.13.106, CYP170A1) is an enzyme with systematic name (+)-epi-isozizaene,NADPH:oxygen oxidoreductase (5-hydroxylating). This enzyme catalyses the following chemical reaction
(S)-2-hydroxypropylphosphonic acid epoxidase (EC 1.14.19.7, HPP epoxidase, HppE, 2-hydroxypropylphosphonic acid epoxidase, Fom4, (S)-2-hydroxypropylphosphonate epoxidase) is an enzyme with systematic name (S)-2-hydroxypropylphosphonate,NADH:oxygen epoxidase. This enzyme catalyses the following chemical reaction
2-Phospho-L-lactate guanylyltransferase is an enzyme with systematic name GTP:2-phospho-L-lactate guanylyltransferase. This enzyme catalyses the following chemical reaction
2-phospho-L-lactate transferase is an enzyme with systematic name (2S)-lactyl-2-diphospho-5'-guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase. This enzyme catalyses the following chemical reaction
2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) (EC 4.2.1.117) is an enzyme with systematic name (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase (2-methyl-trans-aconitate forming). This enzyme catalyses the following chemical reaction
4-oxalomesaconate tautomerase is an enzyme with systematic name 4-oxalomesaconate keto---enol-isomerase. This enzyme catalyses the following chemical reaction
Chlorophyllide a and Chlorophyllide b are the biosynthetic precursors of chlorophyll a and chlorophyll b respectively. Their propionic acid groups are converted to phytyl esters by the enzyme chlorophyll synthase in the final step of the pathway. Thus the main interest in these chemical compounds has been in the study of chlorophyll biosynthesis in plants, algae and cyanobacteria. Chlorophyllide a is also an intermediate in the biosynthesis of bacteriochlorophylls.