Detail Information for IndEnz0005000736
IED ID IndEnz0005000736
Enzyme Type ID lipase000736
Protein Name Diglucosylglycerate octanoyltransferase
DGG octanoyltransferase
EC 2.3.1.273
Gene Name octT C731_2896
Organism Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycolicibacterium Mycolicibacterium hassiacum Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum)
Enzyme Sequence MSGRRPTLLVFCDSLSYYGPRGGLPADDPRIWPNIVASQLDWDVELIGRVGWTSRDVWWAATQDPRAWAALPRAGAVIFATGGMDSLPSPLPTALRELIRYIRPPWLRRRVRDLYGWLQPRLSPVSRNALPPHLTAEYLEMTRGAIDFNRPGIPVVAALPSVHIADSYGRAHHGREATARAITEWARQHGVVLVDLKAAVADQVLNGRGNPDGIHWNFEAHQAVAELMLKALAEAGVPCR
Enzyme Length 240
Uniprot Accession Number K5BJH8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=(2R)-2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-glycerate + octanoyl-CoA = (2R)-2-O-[6-O-octanoyl-alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-glycerate + CoA; Xref=Rhea:RHEA:56868, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:141056, ChEBI:CHEBI:141058; EC=2.3.1.273; Evidence={ECO:0000269|PubMed:26324178};
DNA Binding
EC Number 2.3.1.273
Enzyme Function FUNCTION: Sugar octanoyltransferase likely involved in the biosynthesis of mycobacterial methylglucose lipopolysaccharide (MGLP). Catalyzes the transfer of an octanoyl group from octanoyl-CoA to the C6 OH of the second glucose in diglucosylglycerate (DGG). Can also use hexanoyl-CoA as acyl donor in vitro. DGG is the preferred acceptor, but to a lesser extent, GG (glucosylglycerate) can be used as substrate. DGG and GG are the two earliest intermediates in MGLP biosynthesis. {ECO:0000269|PubMed:26324178}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Activity sharply decreases above this temperature. {ECO:0000269|PubMed:26324178};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:26324178};
Pathway
nucleotide Binding
Features Chain (1)
Keywords Acyltransferase;Reference proteome;Transferase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 26,579
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.5 mM for diglucosylglycerate (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; KM=6.6 mM for glucosylglycerate (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; KM=0.06 mM for octanoyl-CoA (when DGG is used as cosubstrate, at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; KM=0.01 uM for octanoyl-CoA (when GG is used as cosubstrate, at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; KM=0.02 uM for hexanoyl-CoA (when DGG is used as cosubstrate, at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; KM=0.01 uM for hexanoyl-CoA (when GG is used as cosubstrate, at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; Vmax=134 nmol/min/mg enzyme with diglucosylglycerate and octanoyl-CoA as substrates (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; Vmax=32 nmol/min/mg enzyme with glucosylglycerate and octanoyl-CoA as substrates (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178}; Vmax=41 nmol/min/mg enzyme with diglucosylglycerate and hexanoyl-CoA as substrates (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178};
Metal Binding
Rhea ID RHEA:56868
Cross Reference Brenda 2.3.1.273;