| IED ID | IndEnz0001000438 |
| Enzyme Type ID | amylase000438 |
| Protein Name |
Amylosucrase EC 2.4.1.4 |
| Gene Name | ams |
| Organism | Neisseria polysaccharea |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Neisseriales Neisseriaceae Neisseria Neisseria polysaccharea |
| Enzyme Sequence | MLTPTQQVGLILQYLKTRILDIYTPEQRAGIEKSEDWRQFSRRMDTHFPKLMNELDSVYGNNEALLPMLEMLLAQAWQSYSQRNSSLKDIDIARENNPDWILSNKQVGGVCYVDLFAGDLKGLKDKIPYFQELGLTYLHLMPLFKCPEGKSDGGYAVSSYRDVNPALGTIGDLREVIAALHEAGISAVVDFIFNHTSNEHEWAQRCAAGDPLFDNFYYIFPDRRMPDQYDRTLREIFPDQHPGGFSQLEDGRWVWTTFNSFQWDLNYSNPWVFRAMAGEMLFLANLGVDILRMDAVAFIWKQMGTSCENLPQAHALIRAFNAVMRIAAPAVFFKSEAIVHPDQVVQYIGQDECQIGYNPLQMALLWNTLATREVNLLHQALTYRHNLPEHTAWVNYVRSHDDIGWTFADEDAAYLGISGYDHRQFLNRFFVNRFDGSFARGVPFQYNPSTGDCRVSGTAAALVGLAQDDPHAVDRIKLLYSIALSTGGLPLIYLGDEVGTLNDDDWSQDSNKSDDSRWAHRPRYNEALYAQRNDPSTAAGQIYQGLRHMIAVRQSNPRFDGGRLVTFNTNNKHIIGYIRNNALLAFGNFSEYPQTVTAHTLQAMPFKAHDLIGGKTVSLNQDLTLQPYQVMWLEIA |
| Enzyme Length | 636 |
| Uniprot Accession Number | Q9ZEU2 |
| Absorption | |
| Active Site | ACT_SITE 294; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:15023061, ECO:0000305|PubMed:10828446"; ACT_SITE 336; /note="Proton donor"; /evidence="ECO:0000305|PubMed:10828446" |
| Activity Regulation | ACTIVITY REGULATION: Amylosucrase favors hydrolysis at low sucrose concentrations, and polymerization at high sucrose concentrations. Competitively inhibited by fructose. |
| Binding Site | BINDING 152; /note="Substrate"; /evidence="ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"; BINDING 195; /note="Substrate"; /evidence="ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"; BINDING 262; /note="Substrate"; /evidence="ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"; BINDING 292; /note="Substrate"; /evidence="ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"; BINDING 400; /note="Substrate"; /evidence="ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"; BINDING 401; /note="Substrate"; /evidence="ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"; BINDING 517; /note="Substrate"; /evidence="ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + sucrose = [(1->4)-alpha-D-glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:24572, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15444, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721; EC=2.4.1.4; Evidence={ECO:0000269|PubMed:10767427, ECO:0000269|PubMed:10828446}; |
| DNA Binding | |
| EC Number | 2.4.1.4 |
| Enzyme Function | FUNCTION: Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose. {ECO:0000269|PubMed:9882648}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (27); Binding site (7); Chain (1); Frameshift (1); Helix (32); Mutagenesis (7); Sequence conflict (16); Site (1); Turn (11) |
| Keywords | 3D-structure;Direct protein sequencing;Glycosyltransferase;Secreted;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9150231}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (17) |
| Cross Reference PDB | 1G5A; 1JG9; 1JGI; 1MVY; 1MW0; 1MW1; 1MW2; 1MW3; 1S46; 1ZS2; 3UEQ; 4FLO; 4FLQ; 4FLR; 4FLS; 5N6V; 5N7J; |
| Mapped Pubmed ID | 22210773; 23072374; 28732882; |
| Motif | |
| Gene Encoded By | |
| Mass | 72,344 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for sucrose (in the sucrose consumption assay, when initial sucrose < 20 mM) {ECO:0000269|PubMed:10767427}; KM=1.7 mM for sucrose (in the sucrose hydrolysis reaction, when initial sucrose < 20 mM) {ECO:0000269|PubMed:10767427}; KM=1.9 mM for sucrose (in the polymerization reaction, when initial sucrose < 20 mM) {ECO:0000269|PubMed:10767427}; KM=50.2 mM for sucrose (in the sucrose consumption assay, when initial sucrose > 20 mM) {ECO:0000269|PubMed:10767427}; KM=38.7 mM for sucrose (in the sucrose hydrolysis reaction, when initial sucrose > 20 mM) {ECO:0000269|PubMed:10767427}; Vmax=470 umol/min/g enzyme for sucrose consumption (when initial sucrose < 20 mM) {ECO:0000269|PubMed:10767427}; Vmax=288 umol/min/g enzyme for sucrose hydrolysis (when initial sucrose < 20 mM) {ECO:0000269|PubMed:10767427}; Vmax=147 umol/min/g enzyme for polymerization reaction (when initial sucrose < 20 mM) {ECO:0000269|PubMed:10767427}; Vmax=1100 umol/min/g enzyme for sucrose consumption (when initial sucrose > 20 mM) {ECO:0000269|PubMed:10767427}; Vmax=472 umol/min/g enzyme for sucrose hydrolysis (when initial sucrose > 20 mM) {ECO:0000269|PubMed:10767427}; Vmax=1620 umol/min/g enzyme for polymerization reaction (when initial sucrose > 20 mM) {ECO:0000269|PubMed:10767427}; Note=This enzyme does not present a classic Michaelis-Menten behavior for sucrose consumption, that could be related to the presence of a second sucrose binding site. Nevertheless, it is possible to model sucrose consumption rate versus sucrose concentration by two different Michaelis-Menten equations whose apparent kinetic constants are given just above.; |
| Metal Binding | |
| Rhea ID | RHEA:24572 |
| Cross Reference Brenda | 2.4.1.4; |