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1.3.99.15 BENZOYL-COA REDUCTASE.
(CC: -!- REDUCED METHYL VIOLOGEN CAN ACT AS ELECTRON DONOR.
-!- INACTIVE TOWARDS AROMATIC ACIDS THAT ARE NOT COA ESTERS BUT WILL
ALSO CATALYSE THE REACTION: AMMONIA + ACCEPTOR + 2 ADP + 2 PHOSPHATE
+ H(2)O = HYDROXYLAMINE + REDUCED ACCEPTOR + 2 ATP.
-!- IN THE PRESENCE OF REDUCED ACCEPTOR BUT IN THE ABSENCE OF OXIDIZABLE
SUBSTRATE THE ENZYME CATALYSES THE HYDROLYSIS OF ATP TO ADP PLUS
PHOSPHATE.)
2.3.2.9 AGARITINE GAMMA-GLUTAMYLTRANSFERASE.
(CC: -!- 4-HYDROXYANILINE, CYCLOHEXYLAMINE, 1-NAPHTHYLHYDRAZINE AND SIMILAR
COMPOUNDS CAN ACT AS ACCEPTORS.
-!- ALSO CATALYSES THE HYDROLYSIS OF AGARITINE.)
3.1.1.71 ACETYLALKYLGLYCEROL ACETYLHYDROLASE.
(CC: -!- HYDROLYSIS OF THE ACETATE GROUP FROM THE 1,2- AND 1,3- ISOMERS OF
ACETYLALKYLGLYCEROL OCCURS AT APPARENTLY IDENTICAL RATES.
-!- DIFFERS FROM LIPOPROTEIN LIPASE (EC 3.1.1.34) SINCE 1,2-DIACETYL-
SN-GLYCEROLS ARE NOT SUBSTRATES. IT ALSO DIFFERS FROM EC 3.1.1.47
(2-ACETYL-1-ALKYL-GLYCEROPHOSPHOCHOLINE ESTERASE).)
3.1.1.72 ACETYLXYLAN ESTERASE.
(CC: -!- CATALYSES THE HYDROLYSIS OF ACETYL GROUPS FROM POLYMERIC XYLAN,
ACETYLATED XYLOSE, ACETYLATED GLUSOSE, ALPHA-NAPTHYL ACETATE,
P-NITROPHENYL ACETATE BUT NOT FROM TRIACETATYLGLYCEROL.
-!- DOES NOT ACT ON ACETYLATED MANNAN OR PECTIN.)
3.1.2.16 CITRATE (PRO-3S)-LYASE THIOLESTERASE.
(CC: -!- HYDROLYSIS BY THIS ENZYME INACTIVATES EC 4.1.3.6.)
3.1.4.1 PHOSPHODIESTERASE I.
(CC: -!- LOW ACTIVITY TOWARDS POLYNUCLEOTIDES.
-!- A 3'-PHOSPHATE TERMINUS ON THE SUBSTRATE INHIBITS HYDROLYSIS.)
3.1.4.47 VARIANT-SURFACE-GLYCOPROTEIN PHOSPHOLIPASE C.
(CC: -!- BY HYDROLYSIS OF THE ATTACHED GLYCOLIPID, RELEASES SOLUBLE VARIANT-
SURFACE-GLYCOPROTEIN CONTAINING PHOSPHOINOSITOL FROM THE CELL WALL
OF TRYPANOSOMA BRUCEI AFTER CELL LYSIS.
-!- HIGHLY SPECIFIC FOR THE BOUND FORM; ACTS VERY SLOWLY ON FREE 1,2-
DIDECANOYL-SN-PHOSPHATIDYLINOSITOL.
-!- NOT IDENTICAL WITH EC 3.1.4.50.)
3.1.4.50 GLYCOPROTEIN PHOSPHOLIPASE D.
(CC: -!- BY HYDROLYSIS, DEGRADES THE GLYCOSYLPHOSPHATIDYLINOSITOL MEMBRANE
ANCHOR OF CELL-SURFACE PROTEINS IN ANIMAL TISSUES, THUS RELEASING
THESE PROTEINS FROM THE MEMBRANE.
-!- NOT IDENTICAL WITH EC 3.1.4.47.)
3.2.1.20 ALPHA-GLUCOSIDASE.
(CC: -!- GROUP OF ENZYMES WHOSE SPECIFICITY IS DIRECTED MAINLY TOWARDS THE
EXOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC LINKAGES, AND THAT HYDROLYSE
OLIGOSACCHARIDES RAPIDLY, RELATIVE TO POLYSACCHARIDES, WHICH ARE
HYDROLYSED RELATIVELY SLOWLY, OR NOT AT ALL.
-!- THE INTESTINAL ENZYME ALSO HYDROLYSES POLYSACCHARIDES, CATALYSING
THE REACTIONS OF EC 3.2.1.3, AND, MORE SLOWLY, HYDROLYSES 1,6-ALPHA-
D-GLUCOSE LINKS.)
3.2.1.61 MYCODEXTRANASE.
(CC: -!- PRODUCTS ARE NIGEROSE AND 4-ALPHA-D-NIGEROSYLGLUCOSE.
-!- NO HYDROLYSIS OF ALPHA-D-GLUCANS CONTAINING ONLY 1,3- OR 1,4-BONDS.)
3.2.1.128 GLYCYRRHIZINATE BETA-GLUCURONIDASE.
(CC: -!- THE ENZYME FROM ASPERGILLUS NIGER IS SPECIFIC FOR THE HYDROLYSIS OF
THE TRITERPENOID GLYCOSIDE GLYCYRRHIZINATE FROM ROOTS OF GLYCYRRHIZA
SP.)
3.2.1.134 DIFRUCTOSE-ANHYDRIDE SYNTHASE.
(CC: -!- PRODUCES DIFRUCTOSE ANHYDRIDE BY THE REVERSE REACTION OF PARTIAL
HYDROLYSIS, FORMING AN ALPHA-FRUCTOSIDIC LINKAGE.)
3.4.11.3 CYSTINYL AMINOPEPTIDASE.
(CC: -!- HYDROLYSIS RATES ON A RANGE OF AMINOACYL ARYLAMIDES EXCEED THAT FOR
THE CYSTINYL DERIVATIVE.)
3.4.21.53 ENDOPEPTIDASE LA.
(CC: -!- ATP HYDROLYSIS IS LINKED WITH PEPTIDE BOND HYDROLYSIS.
-!- VANADATE INHIBITS BOTH REACTIONS.
-!- A SIMILAR ENZYME OCCURS IN ANIMAL MITOCHONDRIA.
-!- BELONGS TO PEPTIDASE FAMILY S16.)
3.4.22.34 LEGUMAIN.
(CC: -!- FROM GERMINATING COTYLEDONS OF MUNG BEAN (VIGNA RADIATA) AND GARDEN
BEAN (PHASEOLUS VULGARIS).
-!- THOUGHT TO BE INVOLVED IN THE HYDROLYSIS OF STORED SEED PROTEINS.
-!- BELONGS TO PEPTIDASE FAMILY C13.)
3.4.24.12 ENVELYSIN.
(CC: -!- HYDROLYSIS OF PROTEINS OF THE FERTILIZATION ENVELOPE AND
DIMETHYLCASEIN.
-!- DISSOLVES FERTILIZATION ENVELOPE IN EMBRYOS OF SEA URCHIN.
-!- BELONGS TO PEPTIDASE FAMILY M10B.)
3.5.1.43 PEPTIDYL-GLUTAMINASE.
(CC: -!- SPECIFIC FOR THE HYDROLYSIS OF THE GAMMA-AMIDE OF GLUTAMINE
SUBSTITUTED AT THE ALPHA-AMINO GROUP, E.G. GLYCYL-L-GLUTAMINE,
N-ACETYL-L-GLUTAMINE AND L-LEUCYLGLYCYL-L-GLUTAMINE.)
3.5.1.44 PROTEIN-GLUTAMINE GLUTAMINASE.
(CC: -!- SPECIFIC FOR THE HYDROLYSIS OF THE GAMMA-AMIDE OF GLUTAMINE
SUBSTITUTED AT THE CARBOXYL POSITION OR BOTH THE ALPHA-AMINO AND
CARBOXYL POSITIONS, E.G. L-GLUTAMINYLGLYCINE AND L-PHENYLALANYL-L-
GLUTAMINYLGLYCINE.)
3.5.1.54 ALLOPHANATE HYDROLASE.
(CC: -!- THE YEAST ENZYME (BUT NOT THAT FROM GREEN ALGAE) ALSO CATALYSES THE
REACTION OF EC 6.3.4.6, THUS BRINGING ABOUT THE HYDROLYSIS OF UREA
TO CO(2) AND NH(3) IN THE PRESENCE OF ATP AND BICARBONATE.)
3.5.1.78 GLUTATHIONYLSPERMIDINE AMIDASE.
(CC: -!- TRANSFORMS GLUTATHIONYLSPERMIDINE INTO GLUTATHIONE AND SPERMIDINE.
-!- THE ENZYME FROM E.COLI IS BIFUNCTIONAL AND ALSO CATALYSES THE
GLUTATHIONYLSPERMIDINE SYNTHASE (EC 6.3.1.8) REACTION RESULTING IN A
NET HYDROLYSIS OF ATP.)
3.5.4.16 GTP CYCLOHYDROLASE I.
(CC: -!- THE REACTION INVOLVES HYDROLYSIS OF TWO C-N-BONDS AND ISOMERIZATION
OF THE PENTOSE UNIT; THE RECYCLIZATION MAY BE NON-ENZYMIC.)
3.5.4.25 GTP CYCLOHYDROLASE II.
(CC: -!- TWO C-N BONDS ARE HYDROLYSED, RELEASING FORMATE, WITH SIMULTANEOUS
HYDROLYSIS OF THE TERMINAL PYROPHOSPHATE.)
3.6.1.18 FAD PYROPHOSPHATASE.
(CC: -!- THE PLANT ENZYME ALSO HYDROLYSES NAD(+) AND NADH.
-!- THE ANIMAL ENZYME HYDROLYSES NAD AND COA AT ABOUT HALF OF THE RATE
OF HYDROLYSIS OF FAD.
-!- MAY BE IDENTICAL WITH EC 3.6.1.9.)
3.6.1.36 HYDROGEN/POTASSIUM-EXCHANGING ATPASE.
(CC: -!- HYDROLYSIS OF ATP IS COUPLED WITH THE EXCHANGE OF H(+) AND K(+)
IONS.
-!- SO FAR CHARACTERIZED ONLY IN GASTRIC MUCOSA.)
3.6.1.37 SODIUM/POTASSIUM-TRANSPORTING ATPASE.
(CC: -!- AN ENZYME FROM THE PLASMA MEMBRANE OF ANIMAL CELLS.
-!- HYDROLYSIS OF ATP IS COUPLED WITH THE EXCHANGE OF NA(+) AND K(+)
IONS, AND IS SPECIFICALLY INHIBITED BY OUABAIN.)
3.6.1.38 CALCIUM-TRANSPORTING ATPASE.
(CC: -!- HYDROLYSIS OF ATP IS COUPLED WITH THE TRANSPORT OF CA(2+) IONS.
-!- THE ENZYME FROM THE PLASMA MEMBRANE OF EUKARYOTES DIFFERS FROM THAT
FOUND IN SARCOPLASMIC RETICULUM IN THAT IT IS ACTIVATED BY
CALMODULIN, IS SENSITIVE TO LOW CONCENTRATIONS OF VANADATE, AND IS
OF HIGHER MOLECULAR MASS (150 KD).)
4.2.99.18 DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE.
(CC: -!- NICKING OF THE PHOSPHODIESTER BOND IS DUE TO A LYASE-TYPE REACTION,
NOT HYDROLYSIS.
-!- THIS GROUP OF ENZYMES WAS PREVIOUSLY LISTED AS ENDONUCLEASES,
UNDER THE NUMBER EC 3.1.25.2.)
5.99.1.3 DNA TOPOISOMERASE (ATP-HYDROLYSING).
(CC: -!- CAN INTRODUCE NEGATIVE SUPERHELICAL TURNS INTO DOUBLE-STRANDED
CIRCULAR DNA.
-!- ONE UNIT HAS NICKING-CLOSING ACTIVITY, AND ANOTHER CATALYSES
SUPER-TWISTING AND HYDROLYSIS OF ATP (CF. EC 5.99.1.2).)
6.3.4.6 UREA CARBOXYLASE.
(CC: -!- THE YEAST ENZYME (BUT NOT THAT FROM GREEN ALGAE) ALSO CATALYSES THE
REACTION OF EC 3.5.1.54, THUS BRINGING ABOUT THE HYDROLYSIS OF UREA
TO CO(2) AND NH(3).)
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