Anti-codon is complementary to the MRNA Codon
Answer:1. Pyruvate carboxylase
2. Phosphoenol pyruvate carboxy kinase
Explanation:
The conversion of pyruvate to phosphoenol pyruvate is catalyzed by two enzymes Pyruvate carboxylase and phosphoenol pyruvate carboxy kinase
1. Pyruvate carboxylase reaction
Pyruvate in the cytoplasm enters the mitochondria. Then, carboxylase of pyruvate to oxaloacetate is catalysed by a mitochondrial enzyme, pyruvate carboxylase. It needs the co-enzymes biotin and ATP.
The oxaloacetate formed has to be transported from the mitochondrial to the cytosol because further reaction of gluconeogenesis are taking place in cytosol.
2. Phoaphoenol pyruvate carboxy kinase (PEPCK)
In the cytoplasm, PEPCK enzyme then converts oxaloacetate to phoaphoenol pyruvate by removing a molecule of CO2. GTP or ITP donates the phosphate group.
The net effect of these two reactions is the conversion of pyruvate to phoaphoenol pyruvate. This circumverts the irreversible step in glycolysis catalyzed by pyruvate kinase (step 9 if glycolysis)
Of course the major needs of a plant is CHLOROPHYLL, because chlorophyll makes the plant green then SUNLIGHT, because the process cant work without energy. Then WATER and CARBON DIOXIDE.
Hoping this could help
Answer:
Decidable approach
Explanation:they need to make sure how to approach
Answer:
- Calcium binds to troponin C
- Troponin T moves tropomyosin and unblocks the binding sites
- Myosin heads join to the actin forming cross-bridges
- ATP turns into ADP and inorganic phosphate and releases energy
- The energy is used to impulse myofilaments slide producing a power stroke
- ADP is released and a new ATP joins the myosin heads and breaks the bindings to the actin filament
- ATP splits into ADP and phosphate, and the energy produced is accumulated in the myosin heads, starting a new cycle
- Z-bands are pulled toward each other, shortening the sarcomere and the I-band, producing muscle fiber contraction.
Explanation:
In rest, the tropomyosin inhibits the attraction strengths between myosin and actin filaments. Contraction initiates when an action potential depolarizes the inner portion of the muscle fiber. Calcium channels activate in the T tubules membrane, releasing <u>calcium into the sarcolemma.</u> At this point, tropomyosin is obstructing binding sites for myosin on the thin filament. When calcium binds to troponin C, troponin T alters the tropomyosin position by moving it and unblocking the binding sites. Myosin heads join to the uncovered actin-binding points forming cross-bridges, and while doing so, ATP turns into ADP and inorganic phosphate, which is released. Myofilaments slide impulsed by chemical energy collected in myosin heads, producing a power stroke. The power stroke initiates when the myosin cross-bridge binds to actin. As they slide, ADP molecules are released. A new ATP links to myosin heads and breaks the bindings to the actin filament. Then ATP splits into ADP and phosphate, and the energy produced is accumulated in the myosin heads, which starts a new binding cycle to actin. Finally, Z-bands are pulled toward each other, shortening the sarcomere and the I-band, producing muscle fiber contraction.
