CALVIN BENSON CYCLE
Phospho glycerate kinase
EC = 2.7.2.3
Reaction - In the cycle PGK is the seventh enzyme. Catalyses the reaction of 1,3-Biphosphoglycerate and ADP to form 3-Phosphoglycerate and ATP.
Cofactor - 2,3-DPG act as a cofactor which is in the traces in majority cells.
Regulation -
1) Several multivalent anions of low concentrations like sulphate, phosphate, citrate and pyrophosphate activate the enzyme. High concentrations of Mg2+ prohibits the enzyme in a non competitive manner.
2) Salicilates inhibits the activity of PGK, and appeared as a copycat of enzyme's nucleotide substrate because of its prime specification of nuceotide substrate.
3) To increase PGK activity in vitro environments and computer simulations simulating a cell interior, Macromolecular crowding has been indicated. This crowding leads to more compact and enzymatically active enzyme.
Notes - PGK is sequentially conserved in evolution and found in all living organisms. It has a capability of existing in open conformation, gives way to substrate diffusion and products through binding sites.
Glyceraldehyde 3-phosphate dehydrogenase
EC = 1.2.1.12
Reaction - Primary Reaction is glyceraldehyde 3-phosphate (G3P) oxidises in position -1 shows that aldehyde gets transformed to carboxylic acid and reduction of NAD+ is happened concurrently to NADH.
Go' kJ/mol = -50 kJ/mol (12 kcal/mol))
Cofactors - NADH and NAD
Regulation - Allosteric Regulation's morpheein model is used by protein
Notes - Glyceraldehyde -3- phosphate dehydrogenase is a main enzyme in glycolysis which catalyzes pathway firststep and get converted into 3-phospho-D-glyceroyl phosphate.
Nuclear events such as RNA Transport, Transcription, apoptosis and DNA Replication includes GAPDH participation.
Triose Phosphate isomerase
EC = 5.3.1.1
Reaction - The Enzyme Triose phosphate isomerase leads to the catalysation reaction of the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D- glyceraldehyde 3-phosphate.
cofactors - As Triose Phosphate isomerase is an ubiquitous enzyme, the isomerisation reaction takesplace without any cofactors.
Regulation - The regulation is not in a precise manner, whereas before two steps the enzyme is in the phosphofructokinase, glycolytic pathway, irreversible enzyme and highly regulated.
Notes - 1) It is identified in every mammals, organisms, insects, bacteria, fungi and plants.
2) The Deficiency of Triose phosphate isomerase is an autosomal recessive or glycolsis
Aldolase
EC - 4.1.2.13
Reaction - Aldolase can also be mentioned as Fructose biphosphate aldolase, splitting of fructose 1,6-biphosphate, aldol into triose phosphates dihydroxyacetone phosphate and glyceraldehyde 3-phosphate.
Cofactor - Lack of bivalent metal cofactor, class 1 aldolase present in higher plant tissue and animals.
Regulation - Regulation of Aldolase C is primarily due to the gene expression - the mRNA concentration in the cytoplasm. which is also known as adenosine 3', 5' - cyclimonophophate. It will change the gene expression.
Notes - The enzyme Aldolase converts sugar into energy. when a person has muscle damage, aldolase level in the blood increases.
Fructose, 1-6, - biphosphatase
EC - 3.1.3.11
Reaction - Conversion of fructose 1,6 - biphosphate to fructose 6-phosphate ,Catalysation takes place by phosphofructokinase in glycolysis.
Regulation - The enzyme is highly regulated by fructose 2,6 - biphosphate
Calvin-Benson Cycle AG0 (kJ/mol) +70.0 Reaction Ribulose-1,5-bisphosphate CO2 H2O 2(3-phosphoglycerate) +H Enzyme Ribulose-1,5-bisphosphate carboxylase oxygenase ЕС...
The fixation of CO2 into carbohydrates is catalyzed by Select one: a. ribulose 1,5-bisphosphate carboxylase b. thioredoxin c. rubisco activase d. 3-phosphoglycerate