Module 07: Vitamins (Stoker) Flashcards
These are organic compounds that cannot be synthesized in enough amounts by the human body and must be obtained from dietary sources. They are sometimes cofactors in some conjugated enzymes.
Vitamins
In what kind of quantities are vitamins measured?
Micro and Milligram quantities
What are the two generic families of vitamins?
(1) Water Soluble Vitamins
(2) Fat Soluble Vitamins
What is the difference between water soluble vitamins and fat soluble vitamins in terms of absorption?
Water soluble vitamins: Directly into the blood
Fat soluble vitamins: First enter into the lymph system
What is the difference between water soluble vitamins and fat soluble vitamins in terms of transport?
Water soluble vitamins: They travel without carriers
Fat soluble vitamins: They entail (require) protein carriers
What is the difference between water soluble vitamins and fat soluble vitamins in terms of storage?
Water soluble vitamins: They circulate in water-filled parts of the body
Fat soluble vitamins: They are formed in the cells associated with fat
What is the difference between water soluble vitamins and fat soluble vitamins in terms of excretion?
Water soluble vitamins: They are removed by the kidneys in the form of urine
Fat soluble vitamins: They tend to remain in fat storage sites
What is the difference between water soluble vitamins and fat soluble vitamins in terms of toxicity?
Water soluble vitamins: They are not likely to reach toxic levels when consumed from supplements
Fat soluble vitamins: They are likely to reach toxic levels when consumed from supplements.
What is the difference between water soluble vitamins and fat soluble vitamins in terms of dosage frequency?
Water soluble vitamins: needed frequent doses
Fat soluble vitamins: needed in periodic doses
What is the difference between water soluble vitamins and fat soluble vitamins in terms of coenzymes?
Water soluble vitamins: function as coenzymes
Fat soluble vitamins: do not function as coenzymes
What enzymes participate in the transfer of H+ and e-?
(1) nicotinamide adenine dinucleotide (NAD+) and Nicotinamide adenine dinucleotide phosphate (NADP)
(2) Flavin mononucleotide (FMN) and flavin dinucleotide (FAD)
(3) Coenzyme Q
What carry groups carry acyl group?
(1) Thiamine pyrophosphate (TPP)
(2) Lipoic Acid
(3) Coenzyme A
This carries amino group transfer.
Pyridoxal Phosphate
This is entailed for the activation and transfer of CO2
Biocytin
This is entailed for one carbon group transfer
Tetrahydrofolic acid
This carries alkyl groups.
Cobamide coenzyme
How is NADH reduced to NADPH?
(a) Nicotinamide adenine dinucleotide, NAD+, and its phosphorylated analog NADP+ undergo reduction to NADH and NADPH, accepting a hydride ion (two electrons and one proton) from an oxidizable substrate. The hydride ion is added to either the front (the A side) or the back (the B side) of the planar nicotinamide ring.
What is the reduced form of NAD?
nicotinamide adenine dinucleotide phosphate (NADPH)
What is the oxidized form of NADPH?
nicotinamide adenine dinucleotide (NAD+)
NAD and NADP are coenzyme forms of what?
Niacin (Vitamin B3)
What are the reactions involving nicotinamide adenine dinucleotide (NAD+)
lactate DH, malate DH, pyruvate DH complex
What are the reactions involving nicotinamide adenine dinucleotide phosphate (NADPH)
glucose-6P-DH and NADPH in fatty acid synthase complex
NADP+ contains what?
contains a P group on 2’C of adenine ribose
This accepts a H-(hydride ion) and a H+ is released to the medium.
nicotinamide adenine dinucleotide (NAD+)
How does nicotinamide adenine dinucleotide (NAD+) participate in redox reactions?
by accepting H- ions
NAD + -dependent dehydrogenases are often involved in ____________.
catabolism
NADP + -dependent dehydrogenases in ______________.
anabolism
How is FADH+ (FMNH+) reduced to FADH2 (FMNH2)?
Oxidized and reduced FAD and FMN. FMN consists of the structure above the dashed line on the FAD (oxidized form). The flavin nucleotides accept two hydrogen atoms (two electrons and two protons), both of which appear in the flavin ring system. When FAD or FMN accepts only one hydrogen atom, the semiquinone, a stable free radical, forms.
This is referred to as the stable free radical, forms.
Semiquinone
FAD and FMN are coenzyme forms of what?
Riboflavin (Vitamin B2)
What are the reactions involved with flavin adenine dinucleotide (FAD)?
succinic acid DH, (CAC), fatty acyl CoA DH
What are the reactions involved with flavin adenine mononucleotide(FAM)?
L-amino acid oxidase
Riboflavin consists of what?
Riboflavin consists of heterocyclic ring isoalloxazine/ flavin and ribitol attached to N10
flavin adenine mononucleotide(FAM) is composed of what?
P group esterified to 5’OH of ribitol
flavin adenine dinucleotide (FAD) is composed of what? flavin adenine dinucleotide (FAD)?
has an adenosine linked by pyrophosphate bridge to riboflavin (ribitol plus flavin)
How is the semiquinone formed?
Both FAD and FMN can accept and donate 2e- in the isoalloxazine ring. The isoalloxazine ring accepts and transfers e- and protons in a stepwise manner forming a semiquinone
How are flavin coenzymes bounded to the enzyme (prosthetic group?
bound lightly or covalently
This is referred to as a a mitochondrial electron carrier (coenzyme Q) (n=4 to 8)
Ubiquinone
This is a lipid soluble component of ETC found in inner mitochondria membrane. It is not a vitamin because it is produced by the body
Ubiquitous
Ubiquitous is involved in what
the conversion of food into energy.
What is the side chain of Ubiquitous
The side chain consists of variable repeating isoprenoid units
What is the oxidized form of Ubiquitous ?
Ubiquinone
What is the reduced form of Ubiquitous?
ubiquinol (hydroquinone)
What is the reaction of Ubiquinone?
NADH + H+ –> CoQH2 (complex I) of the respiratory chain.
This is the activated form of pantothenic acid (Vitamin B5)
Coenzyme A
Coenzyme A participates in what?
in activation reactions through transfer of acyl groups (RC=O-)
What are the reactions related to coenzyme A?
fatty acyl CoA synthase, dihydrolipoyl transacetylase of PDH complex
How does coenzyme a participate in acyl group transfers?
Some coenzymes containing adenosine. The adenosine portion is shaded in light red. Coenzyme A (CoA) functions in acyl group transfer reactions; the acyl group (such as the acetyl or acetoacetyl group) is attached to the CoA through a thioester linkage to the β-mercaptoethylamine moiety.
In what transfer does NAD+ participate in?
Hydride Transfers
In what transfer does FAD participate in?
Electron Transfers
What is the active form of vitamin B12?
adenosine is 5′-deoxyadenosylcobalamin,
In what transfer does adenosine is 5′-deoxyadenosylcobalamin participate in?
in intramolecular group transfers between adjacent carbons.
What is the reactive portion of coenzyme A?
free sulfhydryl at one end of the molecule
What bond can coenzyme A form with acetate and acyl?
Thioester Bond
What is the optimal integrality of Coenzyme A in the Krebs Cycle?
It acts as a fuel for the Krebs cycle.
What is the relationship between fatty acids and coenzyme A?
Fatty acids are activated once attached to Acyl Coenzyme A (CoA)
This is derived from thiamin (vitamin B1) and is used by many carboxylases and oxidative decarboxylases.
Thiamine Pyrophosphate, TPP
What are transketolases?
move 2 carbons at a time between sugars with keto groups
What is the reactive center of Thiamine Pyrophosphate, TPP?
Thiazolium ring (active site at C2 of the thiazole ring. The H at C2 is acidic, ionizes readily, releasing a H+ and forms a carbanion center.)
What kind of transfer is Thiamine Pyrophosphate, TPP involved in?
Transfer of Aldehyde Group
What are the reactions involved to Thiamine Pyrophosphate, TPP?
pyr decarboxylase of pyr DH complex, transketolases
Explain the reaction behind the Thiamine Pyrophosphate, TPP?
(1) The carbanion center binds and transfers active aldehyde and ketol groups
(2) Bonds to R1 and R2 labilized for loss leaving electron on carbonyl group, where there is the low-energy carbanion
What inactivates Thiamine Pyrophosphate, TPP?
It requires Mg+2 for activity. TPP is inactivated by thiaminase which is found in raw fish.
The Pyridoxal Phosphate exists in 2 forms: what kinds?
(1) Pyridoxal P
(2) Pyridoxamine P
This is is the tightly bound coenzyme of aminotransferases / transaminase.
Pyridoxal 5’-phosphate (PLP)
In what kind of transfer is Pyridoxal 5’-phosphate (PLP) involved in?
They are involved in the transfer of amino groups.
Where is Pyridoxal 5’-phosphate (PLP) derived from?
Derived from Vitamin B6/ Pyridoxine, pyridoxal, pyridoxamine
Pyridoxal 5’-phosphate (PLP) is prosthetic group for many amino-acid-related enzymes, particularly __________
transaminases