| IED ID | IndEnz0005000839 |
| Enzyme Type ID | lipase000839 |
| Protein Name |
Rhamnogalacturonan acetylesterase RhgT RGAE EC 3.1.1.- |
| Gene Name | rhgT yesT BSU07020 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MMKKPIQVFLAGDSTVSDCPPHEAPMAGWGQVFGQLFSEGVLVRNHAKGGASTNSFVEEGRLQAIAEHITQGDYLLIQFGHNDQKPRGTKPYSTFQQFLTLFADTAREKGAHPVFVTSVQRRRFDENGRIEHTLGEYPDAMKALAKELDVPVIDLLAKTKVLYEAYGPEESKRLFVWFQPNEHPNYPDGIEDNTHFSEKGAMEVAKLVAEGIEELGLPLKDHLVSREGKEHV |
| Enzyme Length | 232 |
| Uniprot Accession Number | O31523 |
| Absorption | |
| Active Site | ACT_SITE 14; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 191; /evidence=ECO:0000250; ACT_SITE 195; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Almost completely inhibited by diethylpyrocarbonate at 5 mM and completely inhibited by phenylmethylsulfonyl fluoride (PMSF) at 50 mM. Dimethyl phosphite achieves only a 53% inhibition. Also inhibited by metal ions (magnesium, manganese and calcium) and chelating agent (EDTA) at the same level. {ECO:0000269|PubMed:17957779}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. This enzyme has a broad substrate specificity, and shows strong preference for glucose pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA). Also active toward acetylated xylan. {ECO:0000269|PubMed:17449691}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. The enzyme is quite thermostable in the range of 35 to 40 degrees Celsius, and suffering a decrease in thermostability above 45 degrees Celsius. {ECO:0000269|PubMed:17957779}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. The enzyme is more active in the 7.5-9.0 range, achieving a sharp decrease in the activity below pH 7.0. {ECO:0000269|PubMed:17957779}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Hydrolase;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Up-regulated by growth on type I rhamnogalacturonan. {ECO:0000269|PubMed:17449691}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,944 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.0 mM for alpha-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=1.1 mM for beta-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=2.8 mM for p-nitrophenyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=7.1 mM for cephalosporin C (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=9.1 mM for glucose pentaacetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; KM=124.3 mM for 7-aminocephalosporanic acid (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=709 umol/min/mg enzyme with alpha-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=1163 umol/min/mg enzyme with cephalosporin C (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=3917 umol/min/mg enzyme with beta-naphthyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=4360 umol/min/mg enzyme with 7-aminocephalosporanic acid (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=5160 umol/min/mg enzyme with p-nitrophenyl acetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; Vmax=13726 umol/min/mg enzyme with glucose pentaacetate (at 37 degrees Celsius and pH 7.3) {ECO:0000269|PubMed:17957779}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |