can hydrolyze a-1,4-glucoside bonds of starch into monomers, dimers and oligomers (ex: a-amylase)
removes maltose from non-reducing end of amylose
removes glucose from non-reducing end of amylose
pullalanase and isoamylase
debranching enzymes - hydrolyze a-1,6-glucoside bonds of amylopectin and glycogen
removes from non-reducing end
breaks down starch to be utilized as energy and carbon source (a-1,4 only)
hydrolyzes amorphous regions of cellulose to generate dimers (cellobiose)
loosens crystalline structure of cellulose to create more amorphous regions (theorized)
catalyze hydrolysis AB + H2O = A-OH + B-H
adds an inorganic phosphate AB + P = A + B-P (note: No ATP)
first step in pectin degradation - removes methyl group as methanol (Erwinia carotovora)
second step in pectin degradation - breaks down a-1,4-polygalactouronate to galactouronate monomers
second step in chitin degradation - breaks down B-1,4-N-acetylglucosamine to monomers - hydrolyzes chitosan to chitinase (serratia, pseudomonas, bacillus, streptomyces)
first step in chitin degradation - removes acetyl group, creates chitosan
Transport disaccs into cell without the use of ATP. Phosphorylate a monosaccharide of the disaccharide with inorganic phosphate and liberates the other monosacc.
phosphorylates cellobiose to create glucose-1-phosphate and glucose
phosphorylates maltose to create glucose-1-phosphate and glucose
phosphorylates sucrose to create glucose-1-phosphate and glucose
recognize peptide bonds between specific amino acid sequences and hydrolyze them - may be pH specific, alkaline proteinases have the broadest activity - must be extracelular to utilize extracellular polymers for energy
degrade phospholipids or triglycerides into glycerol and fatty acids
break down nucleic acid polymers into nucleotides
phosphorylate things with high energy phosphate donor (ex. ATP)
phosphorylates fructose to fructose-6-p or mannose to mannose-6-p after active transport into cell
phosphorylates fructose-1-p to fructose-1,6-dp after group translocation into cell
converts glucose-1-p to glucose-6-p
Setup step for B-oxidation - forms acyl-CoA from fatty acids and coenzyme-A
Fatty acyl-CoA dehydrogenase
first oxidation reaction in B-ox, forms FADH
second B-ox step: H2O added
third step in B-ox: forms NADH+H
Acyl COA acyltransferase
Last step in B-ox: Acetyl-CoA split off and CoA added to acyl portion
pyruvate to acetyl CoA
amino acid oxidases
Remove amino group from amino acids with low specificity. Use FAD as prosthetic group
Can produce toxic hydrogen peroxide so not all orgs. can use.
Amino acid dehydrogenase
Oxidative deamination. Oxidizes L-alanine to pyruvate or glutamate to 2-ketoglutarate. Uses NAD+ as a prosthetic group.
Highly specific, most organisms use this pw.
Transfers NH2 group of AA to 2-keto acids.
ALL aas can be deaminated with a transaminase working with a dehydrogenase. Most common pathway for amino acid degradation.
Amino acid dehydratase
Works selectively on serine and threonine to remove and amine and a hydroxyl group at the same time.
Aspartate and histidine dehydratases
Remove amine and hydroxyl from aspartate and histidine and add a double bond between carbons 2 and 3.
removes an amino group and a sulfide from methionine and cysteine
converts methionine to homocysteine
can add one molecule of oxygen from O2 to substrate at cytoplasmic membrane
can incorporate both atoms of O from O2 into one substrate