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UniProt functional annotation for P9WQH3 | ||
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| UniProt code: P9WQH3. |
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| Organism: | |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. |
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| Function: | |
Involved in cholesterol degradation. Catalyzes the conversion of propanal to propanoyl-CoA, using NAD(+) and coenzyme A. Has a broad substrate specificity, and can also use acetaldehyde, butyrlaldehyde, isobutyrlaldehyde and pentaldehyde as substrates. {ECO:0000269|PubMed:23614353}. |
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| Catalytic activity: | |
Reaction=CoA + NAD(+) + propanal = H(+) + NADH + propanoyl-CoA; Xref=Rhea:RHEA:36027, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.87; Evidence={ECO:0000269|PubMed:23614353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36028; Evidence={ECO:0000269|PubMed:23614353}; |
| Catalytic activity: | |
Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000255|HAMAP- Rule:MF_01657, ECO:0000269|PubMed:23614353}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23289; Evidence={ECO:0000269|PubMed:23614353}; |
| Activity regulation: | |
Unlike HsaF, HsaG is active both in the presence and absence of its partner enzyme. {ECO:0000269|PubMed:23614353}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=18 mM for acetaldehyde (in the presence of HsaF) {ECO:0000269|PubMed:23614353}; KM=21.3 mM for acetaldehyde (in the absence of HsaF) {ECO:0000269|PubMed:23614353}; KM=15 mM for propanal (in the presence of HsaF) {ECO:0000269|PubMed:23614353}; KM=12.4 mM for propanal (in the absence of HsaF) {ECO:0000269|PubMed:23614353}; KM=10.6 mM for butyrlaldehyde (in the presence of HsaF) {ECO:0000269|PubMed:23614353}; KM=10 mM for isobutyrlaldehyde (in the presence of HsaF) {ECO:0000269|PubMed:23614353}; KM=20 mM for pentaldehyde (in the presence of HsaF) {ECO:0000269|PubMed:23614353}; KM=0.040 mM for coenzyme A (in the presence of HsaF) {ECO:0000269|PubMed:23614353}; KM=0.415 mM for coenzyme A (in the absence of HsaF) {ECO:0000269|PubMed:23614353}; KM=0.022 mM for NAD(+) (in the presence or absence of HsaF) {ECO:0000269|PubMed:23614353}; KM=1.4 mM for NADP(+) (in the presence of HsaF) {ECO:0000269|PubMed:23614353}; Note=kcat is 9.4 sec(-1) with acetaldehyde as substrate (in the presence of HsaF). kcat is 19.0 sec(-1) with acetaldehyde as substrate (in the absence of HsaF). kcat is 11.1 sec(-1) with propanal as substrate (in the presence of HsaF). kcat is 23.8 sec(-1) with propanal as substrate (in the absence of HsaF). kcat is 7.3 sec(-1) with butyrlaldehyde as substrate. kcat is 5.8 sec(-1) with isobutyrlaldehyde as substrate. kcat is 7.8 sec(-1) with pentaldehyde as substrate. kcat is 9.6 sec(-1) with coenzyme A as substrate (in the presence of HsaF). kcat is 15 sec(-1) with coenzyme A as substrate (in the absence of HsaF). kcat is 7.6 sec(-1) with NAD(+) as substrate (in the presence of HsaF). kcat is 3.9 sec(-1) with NAD(+) as substrate (in the absence of HsaF). kcat is 3.4 sec(-1) with NADP(+) as substrate. {ECO:0000269|PubMed:23614353}; |
| Subunit: | |
Monomer. Forms an heterotetramer composed of two aldolase (HsaF) and two dehydrogenase (HsaG) subunits. {ECO:0000269|PubMed:23614353}. |
| Similarity: | |
Belongs to the acetaldehyde dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01657}. |
Annotations taken from UniProtKB at the EBI.