| IED ID | IndEnz0010000431 |
| Enzyme Type ID | esterase000431 |
| Protein Name |
Carboxylesterase NlhH EC 3.1.1.1 NLH-H |
| Gene Name | nlhH lipH Rv1399c |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MTEPTVARPDIDPVLKMLLDTFPVTFTAADGVEVARARLRQLKTPPELLPELRIEERTVGYDGLTDIPVRVYWPPVVRDNLPVVVYYHGGGWSLGGLDTHDPVARAHAVGAQAIVVSVDYRLAPEHPYPAGIDDSWAALRWVGENAAELGGDPSRIAVAGDSAGGNISAVMAQLARDVGGPPLVFQLLWYPTTMADLSLPSFTENADAPILDRDVIDAFLAWYVPGLDISDHTMLPTTLAPGNADLSGLPPAFIGTAEHDPLRDDGACYAELLTAAGVSVELSNEPTMVHGYVNFALVVPAAAEATGRGLAALKRALHA |
| Enzyme Length | 319 |
| Uniprot Accession Number | P9WK87 |
| Absorption | |
| Active Site | ACT_SITE 162; /evidence=ECO:0000250|UniProtKB:O06350; ACT_SITE 260; /evidence=ECO:0000250|UniProtKB:O06350; ACT_SITE 290; /evidence=ECO:0000250|UniProtKB:O06350 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by diethyl paranitrophenyl phosphate, which is a specific inhibitor of serine hydrolases. {ECO:0000269|PubMed:15373841}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:15373841};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21165; Evidence={ECO:0000269|PubMed:15373841}; CATALYTIC ACTIVITY: Reaction=a propanoate ester + H2O = an aliphatic alcohol + H(+) + propanoate; Xref=Rhea:RHEA:48484, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:36243; Evidence={ECO:0000269|PubMed:15373841};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48485; Evidence={ECO:0000269|PubMed:15373841}; CATALYTIC ACTIVITY: Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+) + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153, ChEBI:CHEBI:88155; Evidence={ECO:0000269|PubMed:15373841};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025; Evidence={ECO:0000269|PubMed:15373841}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:15373841};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:15373841}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:15373841};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000269|PubMed:15373841}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:15373841};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000269|PubMed:15373841}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | FUNCTION: Hydrolyzes various short-chain esters, such as triacylglycerols and vinyl esters. Has no activity against emulsified substrates. {ECO:0000269|PubMed:15373841}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:15373841}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:15373841}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Initiator methionine (1); Modified residue (1); Motif (1) |
| Keywords | Acetylation;Hydrolase;Reference proteome;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note=N-acetylthreonine; /evidence=ECO:0007744|PubMed:21969609 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 88..90; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
| Gene Encoded By | |
| Mass | 33,906 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21164; RHEA:21165; RHEA:48484; RHEA:48485; RHEA:48024; RHEA:48025; RHEA:47348; RHEA:47349; RHEA:12957; RHEA:12958; RHEA:40475; RHEA:40476 |
| Cross Reference Brenda |