MicroPhys- Ch.7 enzymes

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

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)

degrade 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

rearrange things

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

first oxidation reaction in B-ox, forms FADH

second B-ox step: H2O added

third step in B-ox: forms NADH+H

Last step in B-ox: Acetyl-CoA split off and CoA added to acyl portion

pyruvate to acetyl CoA

• 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.

• 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.

Works selectively on serine and threonine to remove and amine and a hydroxyl group at the same time.

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

oxidizes a secondary alcohol to a ketone

oxidizes butanediol to acetoin (a ketone)

oxidizes acetoin to acetyl aldehyde and acetyl CoA

oxidize things (oxidation is loss)

oxidize primary alcohols and aldehydes to fatty acids

oxidizes methane to methanol using NADH as a cosubstrate

reduces pyrollquinoline quinone coupled to the oxidation of methanol to formaldehyde

oxidize formaldehyde in the free form to CO2 via formate

oxidizes bound formaldehyde to CO2

oxidizes bound formaldehyde to CO2 (gram negative methanogens)