Gene Ontology Definition Changes
Files used:
- file 1 (old): 30:09:2011 14:21, cvs revision 1.2291
- file 2 (new): 07:10:2011 17:16, cvs revision 1.2307
- Database: unknown DB type, unknown DB release name
Terms with changed definitions
GO:0008373 : sialyltransferase activity
OLD: Catalysis of the formation of sialylglycoconjugates via transfer of the sialic acid group from CMP to one of several glycoconjugate acceptors.
NEW: Catalysis of the transfer of sialic acid to the terminal portions of the sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins.
GO:0016161 : beta-amylase activity
OLD: Catalysis of the hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
NEW: Catalysis of the reaction: (1,4-alpha-D-glucosyl)(n+1) + H2O = (1,4-alpha-D-glucosyl)(n-1) + alpha-maltose. This reaction is the hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
GO:0018537 : coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity
OLD: Catalysis of the reaction: 5-methyltetrahydromethanopterin + coenzyme F420 + H(+) = 1,5-dihydrocoenzyme F420 + 5,10-methylenetetrahydromethanopterin. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F(420).
NEW: Catalysis of the reaction: 5-methyltetrahydromethanopterin + coenzyme F420 + H(+) = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420.
0 annotations
GO:0022809 : mobile ion carrier activity
OLD: This is a type of carrier produced by bacteria. It enable passive transport by shielding the ion that is being transported from the lipid membrane. It carries an ion across the membrane by enclosing the ion and travelling across the membrane. It does not form a fully open pore across the membrane.
NEW: This is a type of carrier produced by bacteria. It enables passive transport by shielding the ion that is being transported from the lipid membrane. It carries an ion across the membrane by enclosing the ion and travelling across the membrane. It does not form a fully open pore across the membrane.
GO:0030268 : methylenetetrahydromethanopterin dehydrogenase activity
OLD: Catalysis of the reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 + 2 H(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + 1,5-dihydrocoenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: 5,10-methylenetetrahydromethanopterin + coenzyme F420 + 2 H(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + reduced coenzyme F420.
GO:0030570 : pectate lyase activity
OLD: Catalysis of the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
NEW: Catalysis of the reaction: a pectate = a pectate + a pectate oligosaccharide with 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate end. This reaction is the eliminative cleavage of pectate to give oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
GO:0031216 : neopullulanase activity
OLD: Catalysis of the hydrolysis of pullulan to panose (6-a-D-glucosylmaltose).
NEW: Catalysis of the hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).
GO:0033588 : Elongator holoenzyme complex
OLD: A heterohexameric protein complex that is involved in tRNA modification, and exerts indirect effects on transcriptional elongation and exocytosis. The complex can associate physically with hyperphosphorylated RNA polymerase II; it contains two discrete heterotrimeric subcomplexes.
NEW: A heterohexameric protein complex that is involved in modification of wobble nucleosides in tRNA, and exerts direct effects on transcriptional elongation and exocytosis. The complex can associate physically with hyperphosphorylated RNA polymerase II; it contains two discrete heterotrimeric subcomplexes.
0 annotations
GO:0033915 : mannan 1,2-(1,3)-alpha-mannosidase activity
OLD: Catalysis of the hydrolysis of 1,2- and 1,3-linkages in yeast mannan, releasing mannose.
NEW: Catalysis of the hydrolysis of 1,2- and 1,3-linkages in mannan, releasing mannose.
0 annotations
GO:0033941 : mannan exo-1,2-1,6-alpha-mannosidase activity
OLD: Catalysis of the hydrolysis of 1,2-alpha-D- and 1,6-alpha-D- linkages in yeast mannan, releasing D-mannose.
NEW: Catalysis of the hydrolysis of 1,2-alpha-D- and 1,6-alpha-D- linkages in mannan, releasing D-mannose.
0 annotations
GO:0033994 : glucuronan lyase activity
OLD: Catalysis of the eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
NEW: Catalysis of the reaction: (1,4)-beta-D-glucuronan = an oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl end + (1,4)-beta-D-glucuronan. This reaction is the eliminative cleavage of (1->4)-beta-D-glucuronans to give oligosaccharides with 4-deoxy-beta-D-gluc-4-enuronosyl groups at their non-reducing ends. Complete degradation of glucuronans results in the formation of tetrasaccharides.
GO:0033995 : anhydrosialidase activity
OLD: Catalysis of the elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.
NEW: Catalysis of the reaction: an N-acetylneuraminate glycoside = 2,7-anhydro-alpha-N-acetylneuraminate + an alpha-sialyl group. This reaction is the elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.
0 annotations
GO:0033996 : levan fructotransferase (DFA-IV-forming) activity
OLD: Catalysis of the production of di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
NEW: Catalysis of the reaction: beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)]n-D-fructofuranoside = beta-D-fructopyranosyl-(2->6)-[D-fructofuranosyl-(2->6)](n-1)-D-fructofuranoside + di-beta-D-fructofuranose 2,6':2',6-dianhydride. This reaction is the production of di-beta-D-fructofuranose 2,6':2',6-dianhydride (DFA IV) by successively eliminating the diminishing (2->6)-beta-D-fructan (levan) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
0 annotations
GO:0033997 : inulin fructotransferase (DFA-I-forming) activity
OLD: Catalysis of the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
NEW: Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose-beta-D-fructofuranose 1,2':1,2'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
0 annotations
GO:0033998 : inulin fructotransferase (DFA-III-forming) activity
OLD: Catalysis of the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
NEW: Catalysis of the reaction: [(2->1)-beta-D-fructosyl](n) = [(2->1)-beta-D-fructosyl](n-1) + alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride. This reaction is the production of alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,3'-dianhydride (DFA III) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
GO:0033999 : chondroitin B lyase activity
OLD: Catalysis of the eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAC-4S).
NEW: Catalysis of the reaction: dermatan sulfate = n 4-deoxy-beta-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine 4-sulfate. This reaction is the eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (DeltaUA-GalNAC-4S). Chondroitin sulfate B is also known as dermatan sulfate.
GO:0034189 : very-low-density lipoprotein particle binding
OLD: Interacting selectively and non-covalently with a low-density lipoprotein particle, a triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm.
NEW: Interacting selectively and non-covalently with a very-low-density lipoprotein particle, a triglyceride-rich lipoprotein particle that is typically composed of APOB100, APOE and APOCs and has a density of about 1.006 g/ml and a diameter of between 20-80 nm.
0 annotations
GO:0034800 : trinitrophenol dihydride denitratase activity
(was TNP dihydride denitratase activity)
OLD: Catalysis of the reaction: TNP dihydride Meisenheimer complex (aci form) = 2,4-DNP hydride Meisenheimer complex + NO2.
NEW: Catalysis of the reaction: trinitrophenol dihydride Meisenheimer complex (aci form) = 2,4-dinitrophenol hydride Meisenheimer complex + NO2. Trinitrophenol is also known as TNP and dinitrophenol is also known as DNP.
0 annotations
GO:0034914 : trinitrophenol hydride denitratase activity
(was TNP hydride denitratase activity)
OLD: Catalysis of the reaction: TNP hydride Meisenheimer complex = 2,4-dinitrophenol + nitrite.
NEW: Catalysis of the reaction: trinitrophenol hydride Meisenheimer complex = 2,4-dinitrophenol + nitrite. Trinitrophenol is also known as TNP.
GO:0035287 : head segmentation
OLD: Partitioning the head anlage into a fixed number of segmental units. The number of segments composing the insect head has long been a subject of debate, but it is generally agreed that there are 6 or 7 segments. From anterior to posterior the head segments are the procephalic segments (labral, (ocular), antennal and intercalary) and the gnathal segments (mandibular, maxillary and labial).
NEW: Partitioning the insect head anlage into a fixed number of segmental units. The number of segments composing the insect head has long been a subject of debate, but it is generally agreed that there are 6 or 7 segments. From anterior to posterior the head segments are the procephalic segments (labral, (ocular), antennal and intercalary) and the gnathal segments (mandibular, maxillary and labial).
GO:0035288 : anterior head segmentation
OLD: Partitioning the head anlage into procephalic (labral, (ocular), antennal and intercalary) segments. The procephalic segments lie anterior to the gnathal (posterior head) segments, and are pattered by different segmentation gene cascades to the abdominal, thoracic and posterior head (gnathal) segments.
NEW: Partitioning the insect head anlage into procephalic (labral, (ocular), antennal and intercalary) segments. The procephalic segments lie anterior to the gnathal (posterior head) segments, and are pattered by different segmentation gene cascades to the abdominal, thoracic and posterior head (gnathal) segments.
GO:0035289 : posterior head segmentation
OLD: Partitioning the posterior region of the head anlage into gnathal (mandibular, maxillary and labial) segments. Unlike the anterior head (procephalic) segments, formation of the posterior head (gnathal) segments occurs by a similar mechanism to trunk segmentation, where a cascade of gap genes, pair-rule genes and segment-polarity genes subdivide the embryo into progressively smaller domains.
NEW: Partitioning the posterior region of the insect head anlage into gnathal (mandibular, maxillary and labial) segments. Unlike the anterior head (procephalic) segments, formation of the posterior head (gnathal) segments occurs by a similar mechanism to trunk segmentation, where a cascade of gap genes, pair-rule genes and segment-polarity genes subdivide the embryo into progressively smaller domains.
GO:0043130 : ubiquitin binding
OLD: Interacting selectively and non-covalently and non-covalently with ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.
NEW: Interacting selectively and non-covalently with ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.
0 annotations
GO:0043738 : reduced coenzyme F420 dehydrogenase activity
OLD: Catalysis of the reaction: methanophenazine + 1,5-dihydrocoenzyme F420 = dihydromethanophenazine + coenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: methanophenazine + reduced coenzyme F420 = dihydromethanophenazine + coenzyme F420.
0 annotations
GO:0043794 : formate dehydrogenase (coenzyme F420) activity
OLD: Catalysis of the reaction: formate + coenzyme F420 = CO2 + 1,5-dihydrocoenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: formate + coenzyme F420 = CO2 + reduced coenzyme F420.
GO:0045135 : poly(beta-D-mannuronate) lyase activity
OLD: Catalysis of the eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends.
NEW: Catalysis of the reaction: polysaccharides containing beta-D-mannuronate residues = oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl end. This reaction is the eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends.
0 annotations
GO:0046567 : aphidicolan-16 beta-ol synthase activity
OLD: Catalysis of the formation of aphidicolan-16 beta-ol from geranylgeranyl diphosphate.
NEW: Catalysis of the reaction: 9-alpha-copalyl diphosphate + H2O = aphidicolan-16-beta-ol + diphosphate.
GO:0046576 : rhamnogalacturonan alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase activity
(was rhamnogalacturonase B activity)
OLD: Catalysis of the cleavage of (1,2)-alpha-L-Rhap-(1,4)-alpha-D-GalpA glycosidic linkage, generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.
NEW: Catalysis of the cleavage of rhamnogalacturonan, generating oligosaccharides of the form alpha-D-us-galacturonic acid-(1,2)-alpha-L-rhamnose-(1,4)-alpha-D-galacturonate-(1,2)-L-rhamnose-(1,2)-alpha-L-rhamnose-p-(1,4)-alpha-D-galacturonic acid, terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.
GO:0047457 : exo-(1,4)-alpha-D-glucan lyase activity
OLD: Catalysis of the reaction: linear alpha-glucan = 1,5-anhydro-D-fructose + beta-D-glucose.
NEW: Catalysis of the reaction: linear alpha-D-glucan = 1,5-anhydro-D-fructose + beta-D-glucose.
GO:0047487 : oligogalacturonide lyase activity
OLD: Catalysis of the reaction: 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate = 25-dehydro-4-deoxy-D-glucuronate.
NEW: Catalysis of the reaction: 4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate.
0 annotations
GO:0047489 : pectate disaccharide-lyase activity
OLD: Catalysis of the eliminative cleavage of 4-(4-deoxy-a-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin.
NEW: Catalysis of the reaction: a pectate = a pectate + 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate. This reaction is the eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin.
GO:0047490 : pectin lyase activity
OLD: Catalysis of the eliminative cleavage of (14)-a-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-a-D-galact-4-enuronosyl groups at their nonreducing ends.
NEW: Catalysis of the reaction: a pectin = an oligosaccharide with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronate end + a pectin. This reaction is the eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their nonreducing ends.
GO:0047491 : poly(alpha-L-guluronate) lyase activity
OLD: Catalysis of the eliminative cleavage of polysaccharides containing a terminal a-L-guluronate group, to give oligopolysaccharides with 4-deoxy-a-L-erythro-hex-4-enuronosyl groups at their nonreducing ends.
NEW: Catalysis of the reaction: polysaccharides containing a terminal alpha-L-guluronate group = oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl end. This reaction is the eliminative cleavage of polysaccharides containing a terminal a-L-guluronate group, to give oligopolysaccharides with 4-deoxy-a-L-erythro-hex-4-enuronosyl groups at their nonreducing ends.
0 annotations
GO:0047492 : xanthan lyase activity
OLD: Catalysis of the eliminative cleavage of the terminal b-D-mannosyl-b-D-1,4-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-a-L-threo-hex-4-enuronosyl group at the terminus of the side-chain.
NEW: Catalysis of the reaction: xanthan = oligosaccharide with 4-deoxy-alpha-L-threo-hex-4-enuronosyl end + pyruvylate mannose. This reaction is the eliminative cleavage of the terminal beta-D-mannosyl-beta-D-1,4-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the side-chain.
GO:0050454 : coenzyme F420 hydrogenase activity
OLD: Catalysis of the reaction: coenzyme F420 + H(2) + H(+) = 1,5-dihydrocoenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F(420).
NEW: Catalysis of the reaction: coenzyme F420 + H(2) + H(+) = reduced coenzyme F420.
GO:0051060 : pullulanase activity
OLD: Catalysis of the hydrolysis of (1,6)-a-D-glucosidic linkages in pullulan [a linear polymer of a-(1,6)-linked maltotriose units] and in amylopectin and glycogen, and the a- and b-limit dextrins of amylopectin and glycogen.
NEW: Catalysis of the hydrolysis of (1,6)-alpha-D-glucosidic linkages in pullulan (a linear polymer of alpha-(1,6)-linked maltotriose units) and in amylopectin and glycogen, and the a- and b-limit dextrins of amylopectin and glycogen.
0 annotations
GO:0052749 : glucose-6-phosphate dehydrogenase (coenzyme F420) activity
OLD: Catalysis of the reaction: beta-D-glucose 6-phosphate + coenzyme F420 + H+ = 6-O-phosphono-D-glucono-1,5-lactone + 1,5-dihydrocoenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: beta-D-glucose 6-phosphate + coenzyme F420 + H+ = 6-O-phosphono-D-glucono-1,5-lactone + reduced coenzyme F420.
0 annotations
GO:0052752 : reduced coenzyme F420:heterodisulfide oxidoreductase activity
OLD: Catalysis of the reaction: 1,5-dihydrocoenzyme F420 + CoB-S-S-CoM = coenzyme F420 + CoM-SH + CoB-SH. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: reduced coenzyme F420 + CoB-S-S-CoM = coenzyme F420 + CoM-SH + CoB-SH.
0 annotations
GO:0052753 : propan-2-ol:coenzyme F420 oxidoreductase activity
OLD: Catalysis of the reaction: propan-2-ol + coenzyme F420 = acetone + 1,5-dihydrocoenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: propan-2-ol + coenzyme F420 = acetone + reduced coenzyme F420.
0 annotations
GO:0052755 : reduced coenzyme F420:quinone oxidoreductase activity
(was reduced coenzyme F420:2,3-dimethyl-1,4-naphthoquinone oxidoreductase activity)
OLD: Catalysis of the reaction: 1,5-dihydrocoenzyme F420 + 2,3-dimethyl-1,4-naphthoquinone = F420 + reduced 2,3-dimethyl-1,4-naphthoquinone. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420, and reduced 2,3-dimethyl-1,4-naphthoquinone is also known as 2,3-dimethyl-1,4-hydronaphthoquinone.
NEW: Catalysis of the reaction: reduced coenzyme F420 + 2,3-dimethyl-1,4-naphthoquinone = coenzyme F420 + reduced 2,3-dimethyl-1,4-naphthoquinone. Reduced 2,3-dimethyl-1,4-naphthoquinone is also known as 2,3-dimethyl-1,4-hydronaphthoquinone.
0 annotations
GO:0052756 : chitobiose phosphorylase activity
(was sulfite reductase (coenzyme F420) activity)
OLD: Catalysis of the reaction: sulfite + 3 1,5-dihydrocoenzyme F420 = hydrogen sulfide + 3 H2O + 3 coenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: chitobiose + phosphate = N-acetyl-D-glucosamine + N-acetyl-alpha-D-glucosamine 1-phosphate. This reaction is the phosphorolysis of chitobiose, (GlcNAc)2, a dimer of beta-1,4-linked glucosamine units.
0 annotations
GO:0052757 : chondroitin hydrolase activity
(was aflatoxin reductase (coenzyme F420) activity)
OLD: Catalysis of the reaction: aflatoxin + 1,5-dihydrocoenzyme F420 = aflatoxin with reduced furanocoumarin moiety + coenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the hydrolysis of hexosaminic linkages in chondroitin, a linear polymer structure composed of the repeating disaccharide unit [->4)-D-glucuronic acid-(1->3)-N-acetyl-D-galactosamine-(1-], also written as [->4GlcUA1->3GalNAc1-].
0 annotations
GO:0052758 : coenzyme F420-dependent 2,4,6-trinitrophenol reductase activity
(was F420H2:NADP+ oxidoreductase activity)
OLD: Catalysis of the reaction: NADP+ + 1,5-dihydrocoenzyme F420 = NADPH + H+ + coenzyme F420. 1,5-dihydrocoenzyme F420 is also known as reduced coenzyme F420.
NEW: Catalysis of the reaction: 2,4,6-trinitrophenol + H- = 2,4,6-trinitrophenol hydride Meisenheimer complex. Coenzyme F420 supplies the hydride (H-) in the reaction.
GO:0070497 : 6-carboxy-5,6,7,8-tetrahydropterin synthase activity
OLD: Catalysis of the reaction: 7,8-dihydroneopterin triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + PPPi.
NEW: Catalysis of the reaction: 7,8-dihydroneopterin triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H+.
0 annotations
GO:0072557 : IPAF inflammasome complex
OLD: A protein complex that consists of four components, NALP1, PYCARD (ASC)(27), caspase-1 and caspase-5, and includes among its functions that of being the primary mediator of susceptibility to anthrax lethal toxin.
NEW: A protein complex that consists of three components, IPAF, NAIP and caspase-1, and includes among its functions the sensing of flagellin derived from Legionella pneumophila, Salmonella typhimurium, Pseudomonas aeruginosa and Shigella flexneri.
GO:0072558 : NLRP1 inflammasome complex
(was NALP1 inflammasome complex)
OLD: A protein complex that consists of three components, NALP3, PYCARD and caspase-1, and includes among its functions the sensing of various stimuli including anti-viral compounds R837 and R848, bacterial mRNA, gout-associated crystals, bacterial toxins derived from Listeria monocytogenes, Staphylococcus aureus and Shigella flexneri.
NEW: A protein complex that consists of two components, NLRP1 (NALP1) and caspase-1 or caspase-5. The exact mechanisms of NLRP1 activation remain obscure, but potassium ion efflux appears to be essential.
0 annotations
GO:0072559 : NLRP3 inflammasome complex
(was NALP3 inflammasome complex)
OLD: A protein complex that consists of three components, IPAF, NAIP and caspase-1, and includes among its functions the sensing of flagellin derived from Legionella pneumophila, Salmonella typhimurium, Pseudomonas aeruginosa and Shigella flexneri.
NEW: A protein complex that consists of three components, NLRP3 (NALP3), PYCARD and caspase-1. It is activated upon exposure to whole pathogens, as well as a number of structurally diverse pathogen- and danger-associated molecular patterns (PAMPs and DAMPs) and environmental irritants. Whole pathogens demonstrated to activate the NLRP3 inflammasome complex include the fungi Candida albicans and Saccharomyces cerevisiae, bacteria that produce pore-forming toxins, including Listeria monocytogenes and Staphylococcus aureus, and viruses such as Sendai virus, adenovirus, and influenza virus.