Tryptophan synthase or tryptophan synthetase is an enzyme that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae. However, it is absent from Animalia. It is typically found as an α2β2 tetramer. The α subunits catalyze the reversible formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The β subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Each α active site is connected to a β active site by a 25 angstrom long hydrophobic channel contained within the enzyme. This facilitates the diffusion of indole formed at α active sites directly to β active sites in a process known as substrate channeling. The active sites of tryptophan synthase are allosterically coupled.
In molecular biology, the protein domain Saccharopine dehydrogenase (SDH), also named Saccharopine reductase, is an enzyme involved in the metabolism of the amino acid lysine, via an intermediate substance called saccharopine. The Saccharopine dehydrogenase enzyme can be classified under EC 1.5.1.7, EC 1.5.1.8, EC 1.5.1.9, and EC 1.5.1.10. It has an important function in lysine metabolism and catalyses a reaction in the alpha-Aminoadipic acid pathway. This pathway is unique to fungal organisms therefore, this molecule could be useful in the search for new antibiotics. This protein family also includes saccharopine dehydrogenase and homospermidine synthase. It is found in prokaryotes, eukaryotes and archaea.
In enzymology, a cyclopropane-fatty-acyl-phospholipid synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction
The enzyme indole-3-glycerol-phosphate lyase catalyzes the chemical reaction
In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-methylcitrate synthase (EC 2.3.3.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase is an enzyme that catalyzes the chemical reaction
The fluorinase enzyme catalyzes the reaction between fluoride ion and the co-factor S-adenosyl-L-methionine to generate L-methionine and 5'-fluoro-5'-deoxyadenosine, the first committed product of the fluorometabolite biosynthesis pathway. The fluorinase was originally isolated from the soil bacterium Streptomyces cattleya, but homologues have since been identified in a number of other bacterial species, including Streptomyces sp. MA37, Nocardia brasiliensis and Actinoplanes sp. N902-109. This is the only known enzyme capable of catalysing the formation of a carbon-fluorine bond, the strongest single bond in organic chemistry.
Indolocarbazoles (ICZs) are a class of compounds that are under current study due to their potential as anti-cancer drugs and the prospective number of derivatives and uses found from the basic backbone alone. First isolated in 1977, a wide range of structures and derivatives have been found or developed throughout the world. Due to the extensive number of structures available, this review will focus on the more important groups here while covering their occurrence, biological activity, biosynthesis, and laboratory synthesis.
3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase is an enzyme with systematic name 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate:NAD+ oxidoreductase. It is produced by the gene hcaB. This enzyme catalyses the following chemical reaction:
7-Chloro-L-tryptophan oxidase (EC 1.4.3.23, RebO) is an enzyme with systematic name 7-chloro-L-tryptophan:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction
Dichloroarcyriaflavin A synthase (EC 1.13.12.17) is an enzyme with systematic name dichlorochromopyrrolate,NADH:oxygen 2,5-oxidoreductase (dichloroarcyriaflavin A-forming). This enzyme catalyses the following chemical reaction
Clavaminate synthase (EC 1.14.11.21, clavaminate synthase 2, clavaminic acid synthase) is an enzyme with systematic name deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction
Tryptophan 7-halogenase (EC 1.14.19.9, PrnA, RebH) is an enzyme with systematic name L-tryptophan:FADH2 oxidoreductase (7-halogenating). This enzyme catalyses the following chemical reaction:
Demethylrebeccamycin-D-glucose O-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:demethylrebeccamycin-D-glucose O-methyltransferase. This enzyme catalyses the following chemical reaction
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase is an enzyme with systematic name L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase. This enzyme catalyses the following chemical reaction
4′-Demethylrebeccamycin synthase (EC 4.3.3.5, arcyriaflavin A N-glycosyltransferase, RebG) is an enzyme with systematic name 4′-demethylrebeccamycin D-glucose-lyase. It catalyses the following chemical reaction
Adenosylcobinamide-phosphate synthase is an enzyme with systematic name adenosylcobyric acid:(R)-1-aminopropan-2-yl phosphate ligase (ADP-forming). This enzyme catalyses the following chemical reaction
