|
|
||
|
|
|
|
|
UniProt functional annotation for Q58673 | ||
|
|
|
|
|
|
||
| UniProt code: Q58673. |
|
||
| Organism: | |
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii). |
| Taxonomy: | |
Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus. |
|
||
|
||
| Function: | |
Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate. {ECO:0000269|PubMed:17449626}. |
|
||
| Catalytic activity: | |
Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate; Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121; EC=4.2.1.33; Evidence={ECO:0000269|PubMed:17449626}; |
| Catalytic activity: | |
Reaction=(3R)-citramalate = 2-methylmaleate + H2O; Xref=Rhea:RHEA:22332, ChEBI:CHEBI:15377, ChEBI:CHEBI:30719, ChEBI:CHEBI:30934; EC=4.2.1.35; Evidence={ECO:0000269|PubMed:17449626}; |
| Catalytic activity: | |
Reaction=2-methylmaleate + H2O = (2R,3S)-3-methylmalate; Xref=Rhea:RHEA:42424, ChEBI:CHEBI:15377, ChEBI:CHEBI:30719, ChEBI:CHEBI:58511; EC=4.2.1.35; Evidence={ECO:0000269|PubMed:17449626}; |
| Catalytic activity: | |
Reaction=(R)-malate = H2O + maleate; Xref=Rhea:RHEA:23692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15588, ChEBI:CHEBI:30780; EC=4.2.1.31; Evidence={ECO:0000269|PubMed:17449626}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=80 uM for 2-methylmaleate {ECO:0000269|PubMed:17449626}; KM=810 uM for (R)-2-methylmalate {ECO:0000269|PubMed:17449626}; KM=1900 uM for racemic 2-isopropylmalate {ECO:0000269|PubMed:17449626}; KM=39 uM for racemic 3-isopropylmalate {ECO:0000269|PubMed:17449626}; KM=400 uM for maleate {ECO:0000269|PubMed:17449626}; Vmax=15 umol/min/mg enzyme for 2-methylmaleate hydration reaction {ECO:0000269|PubMed:17449626}; Vmax=1.5 umol/min/mg enzyme for (R)-2-methylmalate dehydration reaction {ECO:0000269|PubMed:17449626}; Vmax=4.2 umol/min/mg enzyme for 2-isopropylmalate dehydration reaction {ECO:0000269|PubMed:17449626}; Vmax=1.8 umol/min/mg enzyme for 3-isopropylmalate dehydration reaction {ECO:0000269|PubMed:17449626}; Vmax=34 umol/min/mg enzyme for maleate hydration reaction {ECO:0000269|PubMed:17449626}; pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17449626}; Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:17449626}; |
| Pathway: | |
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. |
| Pathway: | |
Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- oxobutanoate from pyruvate: step 2/3. |
| Subunit: | |
Heterotetramer of 2 LeuC and 2 LeuD. The heterotetramer that can be formed in vitro between HacA and LeuD is inactive. {ECO:0000269|PubMed:17449626}. |
| Similarity: | |
Belongs to the LeuD family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.