Red chlorophyll catabolite reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.3.1.80 | ||||||||
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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RCC_reductase | |||||||||
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Identifiers | |||||||||
Symbol | RCC_reductase | ||||||||
Pfam | PF06405 | ||||||||
InterPro | IPR009439 | ||||||||
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In molecular biology, the red chlorophyll catabolite reductase (RCC reductase) family of proteins consists of several red chlorophyll catabolite reductase (RCC reductase) proteins. Red chlorophyll catabolite (RCC) reductase (RCCR) and pheophorbide (Pheide) a oxygenase (PaO) catalyse the key reaction of chlorophyll catabolism, porphyrin macrocycle cleavage of Pheide a to a primary fluorescent catabolite (pFCC). [1]
A chloroplast is a type of membrane-bound organelle known as a plastid that conducts photosynthesis mostly in plant and algal cells. The photosynthetic pigment chlorophyll captures the energy from sunlight, converts it, and stores it in the energy-storage molecules ATP and NADPH while freeing oxygen from water in the cells. The ATP and NADPH is then used to make organic molecules from carbon dioxide in a process known as the Calvin cycle. Chloroplasts carry out a number of other functions, including fatty acid synthesis, amino acid synthesis, and the immune response in plants. The number of chloroplasts per cell varies from one, in unicellular algae, up to 100 in plants like Arabidopsis and wheat.
Chlorophyll is any of several related green pigments found in cyanobacteria and in the chloroplasts of algae and plants. Its name is derived from the Greek words χλωρός, khloros and φύλλον, phyllon ("leaf"). Chlorophyll allow plants to absorb energy from light.
Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins. It contains an α-amino group (which is in the protonated −NH+
3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain lysyl ((CH2)4NH2), classifying it as a basic, charged (at physiological pH), aliphatic amino acid. It is encoded by the codons AAA and AAG. Like almost all other amino acids, the α-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose of this article, lysine will refer to the biologically active enantiomer L-lysine, where the α-carbon is in the S configuration.
Thylakoids are membrane-bound compartments inside chloroplasts and cyanobacteria. They are the site of the light-dependent reactions of photosynthesis. Thylakoids consist of a thylakoid membrane surrounding a thylakoid lumen. Chloroplast thylakoids frequently form stacks of disks referred to as grana. Grana are connected by intergranal or stromal thylakoids, which join granum stacks together as a single functional compartment.
Brassinosteroids are a class of polyhydroxysteroids that have been recognized as a sixth class of plant hormones and may have utility as anticancer drugs for treating endocrine-responsive cancers by inducing apoptosis of cancer cells and inhibiting cancerous growth. These brassinosteroids were first explored during the 1970s when Mitchell et al. reported promotion in stem elongation and cell division by the treatment of organic extracts of rapeseed pollen. Brassinolide was the first brassinosteroid to be isolated in 1979, when pollen from Brassica napus was shown to promote stem elongation and cell divisions, and the biologically active molecule was isolated. The yield of brassinosteroids from 230 kg of Brassica napus pollen was only 10 mg. Since their discovery, over 70 BR compounds have been isolated from plants.
Photosystem I is one of two photosystems in the photosynthetic light reactions of algae, plants, and cyanobacteria. Photosystem I is an integral membrane protein complex that uses light energy to catalyze the transfer of electrons across the thylakoid membrane from plastocyanin to ferredoxin. Ultimately, the electrons that are transferred by Photosystem I are used to produce the moderate-energy hydrogen carrier NADPH. The photon energy absorbed by Photosystem I also produces a proton-motive force that is used to generate ATP. PSI is composed of more than 110 cofactors, significantly more than Photosystem II.
Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.
Catabolite activator protein is a trans-acting transcriptional activator that exists as a homodimer in solution. Each subunit of CAP is composed of a ligand-binding domain at the N-terminus and a DNA-binding domain at the C-terminus. Two cAMP molecules bind dimeric CAP with negative cooperativity. Cyclic AMP functions as an allosteric effector by increasing CAP's affinity for DNA. CAP binds a DNA region upstream from the DNA binding site of RNA Polymerase. CAP activates transcription through protein-protein interactions with the α-subunit of RNA Polymerase. This protein-protein interaction is responsible for (i) catalyzing the formation of the RNAP-promoter closed complex; and (ii) isomerization of the RNAP-promoter complex to the open conformation. CAP's interaction with RNA polymerase causes bending of the DNA near the transcription start site, thus effectively catalyzing the transcription initiation process. CAP's name is derived from its ability to affect transcription of genes involved in many catabolic pathways. For example, when the amount of glucose transported into the cell is low, a cascade of events results in the increase of cytosolic cAMP levels. This increase in cAMP levels is sensed by CAP, which goes on to activate the transcription of many other catabolic genes.
Biological pigments, also known simply as pigments or biochromes, are substances produced by living organisms that have a color resulting from selective color absorption. Biological pigments include plant pigments and flower pigments. Many biological structures, such as skin, eyes, feathers, fur and hair contain pigments such as melanin in specialized cells called chromatophores. In some species, pigments accrue over very long periods during an individual's lifespan.
Autumn leaf color is a phenomenon that affects the normally green leaves of many deciduous trees and shrubs by which they take on, during a few weeks in the autumn season, various shades of yellow, orange, red, purple, and brown. The phenomenon is commonly called autumn colours or autumn foliage in British English and fall colors, fall foliage, or simply foliage in American English.
Chlorophyllase is an essential enzyme in chlorophyll metabolism. It is a membrane proteins commonly known as chlase (EC 3.1.1.14, CLH) with systematic name chlorophyll chlorophyllidohydrolase. It catalyzes the reaction
In enzymology, protochlorophyllide reductases (POR) are enzymes that catalyze the conversion from protochlorophyllide to chlorophyllide a. They are oxidoreductases participating in the biosynthetic pathway to chlorophylls.
In enzymology, a nitrite reductase (NO-forming) (EC 1.7.2.1) is an enzyme that catalyzes the chemical reaction
High-mobility group protein B2 also known as high-mobility group protein 2 (HMG-2) is a protein that in humans is encoded by the HMGB2 gene.
Adrenodoxin reductase, was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis. Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes.
In molecular biology, the KduI/IolB isomerase family is a family of isomerase enzymes that includes 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase (KduI) and 5-deoxy-glucuronate isomerase (IolB).
Chlorophyll(ide) b reductase (EC 1.1.1.294), chlorophyll b reductase, Chl b reductase) is an enzyme with systematic name 71-hydroxychlorophyllide-a:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
Pheophorbide a oxygenase (EC 1.14.15.17, pheide a monooxygenase, pheide a oxygenase, PAO) is an enzyme with systematic name pheophorbide-a,NADPH:oxygen oxidoreductase (biladiene-forming). This enzyme catalyses the following chemical reaction
Philip A. Rea is a British biochemist, science writer and educator, who is currently Professor of Biology and Rebecka and Arie Belldegrun Distinguished Director of the Vagelos Program in Life Sciences & Management at the University of Pennsylvania. His major contributions as a biochemist have been in the areas of membrane transport and xenobiotic detoxification, and as a science writer and educator in understanding the intersection between the life sciences and their implementation. In 2005, he and Mark V. Pauly founded the Roy and Diana Vagelos Program in Life Sciences & Management between the School of Arts and Sciences and Wharton School at the University of Pennsylvania, which he continues to co-direct in his capacity as Belldegrun Distinguished Director. Rea's work on serendipity in science has been featured in The Wall Street Journal. Additionally, he has served as a subject matter expert for 'The Scientist.
Howard Sidney (Sid) Thomas, FWIF, FLSW was a plant scientist at the Welsh Plant Breeding Station and later the University of Aberystwyth, and also a jazz musician and composer. He became Emeritus Professor of Biological, Environmental and Rural Sciences, University of Aberystwyth.