Nutrition Guide

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QT3.

In enzymology, a N-isopropylammelide isopropylaminohydrolase (EC 3.5.99.4) is an enzyme that catalyzes the chemical reaction
N-isopropylammelide + H2O cyanuric acid + isopropylamine

Thus, the two substrates of this enzyme are N-isopropylammelide and H2O, whereas its two products are cyanuric acid and isopropylamine.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is N-isopropylammelide isopropylaminohydrolase. This enzyme is also called AtzC. This enzyme participates in atrazine degradation.

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1J5X, 1JT9, 1NE7, 2BKV, and 2BKX.

In enzymology, a glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an enzyme that catalyzes the chemical reaction
D-glucosamine 6-phosphate + H2O D-fructose 6-phosphate + NH3

Thus, the two substrates of this enzyme are D-glucosamine 6-phosphate and H2O, whereas its two products are D-fructose 6-phosphate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing). Other names in common use include glucosaminephosphate isomerase, glucosamine-6-phosphate isomerase, phosphoglucosaminisomerase, glucosamine phosphate deaminase, aminodeoxyglucosephosphate isomerase, and phosphoglucosamine isomerase. This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 6-phosphate.

In enzymology, a 2-aminomuconate deaminase (EC 3.5.99.5) is an enzyme that catalyzes the chemical reaction
2-aminomuconate + H2O 4-oxalocrotonate + NH3

Thus, the two substrates of this enzyme are 2-aminomuconate and H2O, whereas its two products are 4-oxalocrotonate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-aminomuconate aminohydrolase. This enzyme participates in tryptophan metabolism.

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1RQX, 1TYZ, 1TZ2, 1TZJ, 1TZK, and 1TZM

In enzymology, a 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) is an enzyme that catalyzes the chemical reaction
1-aminocyclopropane-1-carboxylate + H2O 2-oxobutanoate + NH3

Thus, the two substrates of this enzyme are 1-aminocyclopropane-1-carboxylate and H2O, whereas its two products are 2-oxobutanoate and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also called 1-aminocyclopropane-1-carboxylate endolyase (deaminating). This enzyme participates in propanoate metabolism. It employs one cofactor, pyridoxal phosphate.

In enzymology, a phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) is an enzyme that catalyzes the chemical reaction
1-(5-phosphoribosyl)-AMP + H2O 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4-carboxamide

Thus, the two substrates of this enzyme are 1-(5-phosphoribosyl)-AMP and H2O, whereas its two products are [[1-(5-phosphoribosyl)-5-[(5-]] and [[phosphoribosylamino)methylideneamino]imidazole-4-carboxamide]].

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase. Other names in common use include PRAMP-cyclohydrolase, and phosphoribosyladenosine monophosphate cyclohydrolase. This enzyme participates in histidine metabolism.

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1WN5 and 1WN6.

ADA2 is the predominant form present in human blood plasma and is increased in many diseases, particularly those associated with the immune system: for example rheumatoid arthritis, psoriasis and sarcoidosis. The plasma AD2 isoform is also increased in most cancers.

Total plasma ADA can be measured using high performance liquid chromatography, enzymatic or colorimetric techniques. Perhaps the simplest system is the measurement of the ammonia released from adenosine when broken down to inosine. After incubation of plasma with a buffered solution of adenosine the ammonia is reacted with a Berthelot reagent to form a blue colour which is proportionate to the amount of enzyme activity. To measure ADA2, erythro-9-(2-hydroxy-3-nonyl) adenine (EHNA) is added prior to incubation so as to inhibit the enzymatic acivity of ADA1[4]. It is the absence of ADA1 that causes SCID.