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| ID | Date/Time | EC/Citation Key | Table | Field | Changed From | Changed To | |
| 58645 | 2008-08-01 12:11:21 | 3.1.26.12 | html | comments | RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication [1]. The enzyme binds to monophosphorylated 5′ ends of substrates but exhibits sequential cleavages in the 3′ to 5′ direction [1]. 2′-O-Methyl nucleotide substitutions at RNase E binding sites does not prevent binding but does prevent cleavage of non-modified target sequences 5′ to that locus [1]. In Escherichia coli, the enzyme is found in the RNA degradosome. The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, enolase (EC 4.1.1.11) and polynucleotide phosphorylase (EC 2.7.7.8). | RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication [1]. The enzyme binds to monophosphorylated 5′ ends of substrates but exhibits sequential cleavages in the 3′ to 5′ direction [1]. 2′-O-Methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5′ to that locus [1]. In Escherichia coli, the enzyme is found in the RNA degradosome. The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, enolase (EC 4.1.1.11) and polynucleotide phosphorylase (EC 2.7.7.8). | |
| 58643 | 2008-08-01 12:11:21 | 3.1.26.12 | entry | comments | RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication [1]. The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction [1]. 2'-O-Methyl nucleotide substitutions at RNase E binding sites does not prevent binding but does prevent cleavage of non-modified target sequences 5' to that locus [1]. In Escherichia coli, the enzyme is found in the RNA degradosome. The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, enolase (EC 4.1.1.11) and polynucleotide phosphorylase (EC 2.7.7.8). | RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication [1]. The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction [1]. 2'-O-Methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5' to that locus [1]. In Escherichia coli, the enzyme is found in the RNA degradosome. The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, enolase (EC 4.1.1.11) and polynucleotide phosphorylase (EC 2.7.7.8). | |
| 58636 | 2008-08-01 11:59:47 | 1.3.1.81 | html | comments | The reaction occurs in the opposite direction to that shown above. NADH cannot replace NADPH as reductant. The Δ8,9-double bond of (+)-cis-isopulegone and the Δ1,2-double bond of (±)-piperitone are not substrates. The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (-)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyse the reverse reaction. This enzyme is a member of the medium-chain dehydrogenase/reductase superfamily. | NADH cannot replace NADPH as reductant. The Δ8,9-double bond of (+)-cis-isopulegone and the Δ1,2-double bond of (±)-piperitone are not substrates. The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (-)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyse the reverse reaction. This enzyme is a member of the medium-chain dehydrogenase/reductase superfamily. | |
| 58634 | 2008-08-01 11:59:47 | 1.3.1.81 | entry | comments | The reaction occurs in the opposite direction to that shown above. NADH cannot replace NADPH as reductant. The Delta8,9-double bond of (+)-cis-isopulegone and the Delta1,2-double bond of (±)-piperitone are not substrates. The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (-)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyse the reverse reaction. This enzyme is a member of the medium-chain dehydrogenase/reductase superfamily. | NADH cannot replace NADPH as reductant. The Delta8,9-double bond of (+)-cis-isopulegone and the Delta1,2-double bond of (±)-piperitone are not substrates. The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (-)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyse the reverse reaction. This enzyme is a member of the medium-chain dehydrogenase/reductase superfamily. | |
| 58633 | 2008-08-01 11:55:25 | 1.2.1.73 | cite | cite_key | krejcik-z-2008-159 | ||
| 58632 | 2008-08-01 11:55:25 | 1.2.1.73 | cite | ref_num | 1 | ||
| 58618 | 2008-08-01 11:49:57 | 2.4.1.245 | html | comments | Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzyme from the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP and GDP-glucose to the same extent [2], that from Thermococcus litoralis has a marked preference for ADP [1]. | Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzyme from the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-glucose to the same extent [2], that from Thermococcus litoralis has a marked preference for ADP [1]. | |
| 58617 | 2008-08-01 11:49:57 | 2.4.1.245 | html | sys_name | NDP-glucose:D-glucose 1-α-D-glucosyltransferase | ADP-glucose:D-glucose 1-α-D-glucosyltransferase | |
| 58615 | 2008-08-01 11:49:57 | 2.4.1.245 | entry | comments | Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for alpha,alpha-trehalose as substrate, as it cannot use alpha- or beta-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzyme from the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP and GDP-glucose to the same extent [2], that from Thermococcus litoralis has a marked preference for ADP [1]. | Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for alpha,alpha-trehalose as substrate, as it cannot use alpha- or beta-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzyme from the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-glucose to the same extent [2], that from Thermococcus litoralis has a marked preference for ADP [1]. | |
| 58614 | 2008-08-01 11:49:57 | 2.4.1.245 | entry | sys_name | NDP-glucose:D-glucose 1-alpha-D-glucosyltransferase | ADP-glucose:D-glucose 1-alpha-D-glucosyltransferase | |
| 58613 | 2008-07-31 03:17:22 | 3.4.24.85 | html | comments | Type example of peptidase family M50. The transcription factors SREBP-1 and -2 are synthesized as precursor proteins that are attached to the membranes of the endoplasmic reticulum and two cleavages are needed to release the active factor so that it can move to the nucleus. This enzyme cleaves the second of these, and is thus the "site 2 protease", S2P. | Type example of peptidase family M50. The transcription factors SREBP-1 and -2 are synthesized as precursor proteins that are attached to the membranes of the endoplasmic reticulum and two cleavages are needed to release the active factor so that it can move to the nucleus. This enzyme cleaves the second of these, and is thus the "site 2 protease", S2P. | |
| 58612 | 2008-07-31 03:17:22 | 3.4.24.85 | html | reaction | Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site DRSRILL483┼CVLTFLCLSFNPLTSLLQWGGA, in which the membrane-spanning segment is underlined. The residues NP (bold), 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced. | Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site DRSRILL483┼CVLTFLCLSFNPLTSLLQWGGA, in which the membrane-spanning segment is underlined. The residues NP (bold), 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced. | |
| 58611 | 2008-07-31 03:17:22 | 3.4.24.85 | html | accepted_name | S2P endopeptidase | S2P endopeptidase | |
| 58610 | 2008-07-31 03:16:47 | 3.4.24.46 | html | links | BRENDA, ERGO, EXPASY, IUBMB, KEGG, MEROPS, PDB | BRENDA, ERGO, EXPASY, IUBMB, KEGG, MEROPS, PDB | |
| 58609 | 2008-07-31 03:16:47 | 3.4.24.46 | html | comments | From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Two isoenzymes of approx. 24 kDa that inactivate α1-proteinase inhibitor by a single cleavage. In peptidase family M12 (astacin family) | From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Two isoenzymes of approx. 24 kDa that inactivate α1-proteinase inhibitor by a single cleavage. In peptidase family M12 (astacin family) | |
| 58577 | 2008-07-30 16:29:55 | 3.6.4.6 | html | comments | A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome. | A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger’s syndrome. | |
| 58576 | 2008-07-30 16:29:55 | 3.6.4.6 | entry | comments | A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome. | A large family of ATP-hydrolysing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments. They belong to the AAA-type (_A_TPase _a_ssociated with a variety of cell _a_ctivities) ATPase superfamily. They include peroxin, which apparently is involved in Zellweger's syndrome. | |
| 58496 | 2008-07-30 15:22:37 | 3.6.3.13 | hist | note | Aminophospholipid-transporting ATPase. Identical to EC 3.6.3.1, phospholipid-translocating ATPase | aminophospholipid-transporting ATPase. Identical to EC 3.6.3.1, phospholipid-translocating ATPase | |
| 58469 | 2008-07-30 14:58:52 | 3.4.99.32 | hist | note | Armillaria mellea neutral proteinase. Now EC 3.4.24.20 peptidyl-Lys metalloendopeptidase | Armillaria mellea neutral proteinase. Now EC 3.4.24.20, peptidyl-Lys metalloendopeptidase | |