Sirohydrochlorin Ferrochelatase
   HOME
*





Sirohydrochlorin Ferrochelatase
The enzyme sirohydrochlorin ferrochelatase (EC 4.99.1.4) catalyzes the following reaction: : siroheme + 2H+ \rightleftharpoons sirohydrochlorin + Fe2+ This enzyme belongs to the family of lyases, to be specific the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is siroheme ferro-lyase (sirohydrochlorin-forming). The enzyme is also known as SirB and present in all plants and nitrate and sulfate assimilating/dissimilating bacteria. Siroheme is a co-factor of both assimilatory and dissimilatory nitrite and sulfite reductases. Siroheme is synthesized from the central tetrapyrrole molecule uroporphyrinogen III, which forms the first branch-point of tetrapyrrole biosynthetic pathway, the other branch being the heme/chlorophyll branch. The siroheme branch consists of three steps: methylation, dehydrogenation, and ferrochelation, with the last step carried out by sirohydrochlorin ferrochelatase. Sirohydrochlorin ferrochel ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


Siroheme
Siroheme (or sirohaem) is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. It is a cofactor at the active site of sulfite reductase, which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide, which can be incorporated into the organic compound homocysteine. Biosynthesis Like all tetrapyrroles, the macrocyclic ligand in siroheme is derived from uroporphyrinogen III. This porphyrinogen is methylated at two adjacent pyrrole rings to give dihydrosirohydrochlorin, which is subsequently oxidized to give sirohydrochlorin Sirohydrochlorin is a tetrapyrrole macrocyclic metabolic intermediate in the biosynthesis of sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. It is also the biosynthetic precursor to cofactor F430, an enzyme which cat .... A ferrochelatase then inserts iron into the macrocycle to give siroheme. See also * Ferredoxin-nitrite ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Catalysis
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. Estimates are that 90% of all commercially produced chemical products involve catalysts at some s ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


Biochemical Journal
The ''Biochemical Journal'' is a peer-reviewed scientific journal which covers all aspects of biochemistry, as well as cell and molecular biology. It is published by Portland Press and was established in 1906. History The journal was established in 1906 by Benjamin Moore, holder of the first UK chair of biochemistry at the University of Liverpool, with financial support from Edward Whitley, an heir of the Greenall Whitley brewers.Clark J. Biochemical Journal Centenary (2006)
(accessed 30 September 2007)
The two served as the first and the journal was initially published by the

Lyase
In biochemistry, a lyase is an enzyme that catalyzes the breaking (an elimination reaction) of various chemical bonds by means other than hydrolysis (a substitution reaction) and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible (called a Michael reaction). For example, an enzyme that catalyzed this reaction would be a lyase: : ATP → cAMP + PPi Lyases differ from other enzymes in that they require only one substrate for the reaction in one direction, but two substrates for the reverse reaction. Nomenclature Systematic names are formed as "''substrate group-lyase''." Common names include decarboxylase, dehydratase, aldolase, etc. When the product is more important, synthase may be used in the name, e.g. phosphosulfolactate synthase (EC 4.4.1.19, Michael addition of sulfite to phosphoenolpyruvate). A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY or MetZ) which ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  




List Of Enzymes
This article lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system. * List of EC numbers (EC 5) * List of EC numbers (EC 6) :Oxidoreductases (EC 1) (Oxidoreductase) *Dehydrogenase * Luciferase *DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) **Homoserine dehydrogenase ** Aminopropanol oxidoreductase **Diacetyl reductase **Glycerol dehydrogenase **Propanediol-phosphate dehydrogenase ** glycerol-3-phosphate dehydrogenase (NAD+) ** D-xylulose reductase **L-xylulose reductase **Lactate dehydrogenase **Malate dehydrogenase **Isocitrate dehydrogenase ** HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) **Glucose oxidase **L-gulonolactone oxidase **Thiamine oxidase **Xanthine oxidase * :EC 1.1.4 (with a disul ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


Tetrapyrrole
Tetrapyrroles are a class of chemical compounds that contain four pyrrole or pyrrole-like rings. The pyrrole/pyrrole derivatives are linked by ( =- or -- units), in either a linear or a cyclic fashion. Pyrroles are a five-atom ring with four carbon atoms and one nitrogen atom. Tetrapyrroles are common cofactors in biochemistry and their biosynthesis and degradation feature prominently in the chemistry of life. Some tetrapyrroles form the active core of compounds with crucial biochemical roles in living systems, such as hemoglobin and chlorophyll. In these two molecules, in particular, the pyrrole macrocycle ring frames a metal atom, that forms a coordination compound with the pyrroles and plays a central role in the biochemical function of those molecules. Structure Linear tetrapyrroles (called bilanes) include: *Heme breakdown products (e.g., bilirubin, biliverdin) * Phycobilins (found in cyanobacteria) *Luciferins as found in dinoflagellates and euphausiid shrimps (krill) F ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Methylation
In the chemical sciences, methylation denotes the addition of a methyl group on a substrate, or the substitution of an atom (or group) by a methyl group. Methylation is a form of alkylation, with a methyl group replacing a hydrogen atom. These terms are commonly used in chemistry, biochemistry, soil science, and the biological sciences. In biological systems, methylation is catalyzed by enzymes; such methylation can be involved in modification of heavy metals, regulation of gene expression, regulation of protein function, and RNA processing. In vitro methylation of tissue samples is also one method for reducing certain histological staining artifacts. The reverse of methylation is demethylation. In biology In biological systems, methylation is accomplished by enzymes. Methylation can modify heavy metals, regulate gene expression, RNA processing and protein function. It has been recognized as a key process underlying epigenetics. Methanogenesis Methanogenesis, the process th ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Dehydrogenation
In chemistry, dehydrogenation is a chemical reaction that involves the removal of hydrogen, usually from an organic molecule. It is the reverse of hydrogenation. Dehydrogenation is important, both as a useful reaction and a serious problem. At its simplest, it is useful way of converting alkanes, which are relatively inert and thus low-valued, to olefins, which are reactive and thus more valuable. Alkenes are precursors to aldehydes (), alcohols (), polymers, and aromatics. As a problematic reaction, the fouling and inactivation of many catalysts arises via coking, which is the dehydrogenative polymerization of organic substrates. Enzymes that catalyze dehydrogenation are called dehydrogenases. Heterogeneous catalytic routes Styrene Dehydrogenation processes are used extensively to produce aromatics in the petrochemical industry. Such processes are highly endothermic and require temperatures of 500 °C and above. Dehydrogenation also converts saturated fats to unsatura ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Magnesium Chelatase
Magnesium-chelatase is a three-component enzyme () that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of chlorophyll and bacteriochlorophyll. As a result, it is thought that Mg-chelatase has an important role in channeling intermediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth: protoporphyrin IX + + ATP + \rightleftharpoons ADP + phosphate + Mg-protoporphyrin IX + 2 The four substrates of this enzyme are ATP, protoporphyrin IX, Mg2+, and H2O; its four products are ADP, phosphate, Mg-protoporphyrin IX, and H+. This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is Mg-protoporphyrin IX magnesium-lyase. Other names in common use include protoporphyrin IX magnesium-chelatase, protoporphyrin IX Mg-chelatase, magnesium-protoporphyrin IX chelatase, ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Baker's Yeast
Baker's yeast is the common name for the strains of yeast commonly used in baking bread and other bakery products, serving as a leavening agent which causes the bread to rise (expand and become lighter and softer) by converting the fermentable sugars present in the dough into carbon dioxide and ethanol. Baker's yeast is of the species ''Saccharomyces cerevisiae'', and is the same species (but a different strain) as the kind commonly used in alcoholic fermentation, which is called brewer's yeast. Baker's yeast is also a single-cell microorganism found on and around the human body. The use of steamed or boiled potatoes, water from potato boiling, or sugar in a bread dough provides food for the growth of yeasts; however, too much sugar will dehydrate them. Yeast growth is inhibited by both salt and sugar, but more so by salt than sugar. Some sources say fats, such as butter and eggs, slow down yeast growth; others say the effect of fat on dough remains unclear, presenting evidenc ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Land Plants
The Embryophyta (), or land plants, are the most familiar group of green plants that comprise vegetation on Earth. Embryophytes () have a common ancestor with green algae, having emerged within the Phragmoplastophyta clade of green algae as sister of the Zygnematophyceae. The Embryophyta consist of the bryophytes plus the polysporangiophytes. Living embryophytes therefore include hornworts, liverworts, mosses, lycophytes, ferns, gymnosperms and flowering plants. The land plants have diplobiontic life cycles and it is accepted now that they emerged from freshwater, multi-celled algae. The embryophytes are informally called land plants because they live primarily in terrestrial habitats (with exceptional members who evolved to live once again in aquatic habitats), while the related green algae are primarily aquatic. Embryophytes are complex multicellular eukaryotes with specialized reproductive organs. The name derives from their innovative characteristic of nurturing the young ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]  


picture info

Green Algae
The green algae (singular: green alga) are a group consisting of the Prasinodermophyta and its unnamed sister which contains the Chlorophyta and Charophyta/Streptophyta. The land plants (Embryophytes) have emerged deep in the Charophyte alga as sister of the Zygnematophyceae. Since the realization that the Embryophytes emerged within the green algae, some authors are starting to properly include them. The completed clade that includes both green algae and embryophytes is monophyletic and is referred to as the clade Viridiplantae and as the kingdom Plantae. The green algae include unicellular and colonial flagellates, most with two flagella per cell, as well as various colonial, coccoid and filamentous forms, and macroscopic, multicellular seaweeds. There are about 22,000 species of green algae. Many species live most of their lives as single cells, while other species form coenobia (colonies), long filaments, or highly differentiated macroscopic seaweeds. A few other organi ...
[...More Info...]      
[...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]