Property | Value | Creator | Evidence | PMID | Comment |
Term | TBRXN:MYC1M2 Mycolic Acid Methyl Hydroxyl Addition - IDA | njamshidi | IDA | 16356931 | PMID: 16356931 F. Boissier, F. Bardou et al. Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. J. Biol. Chem. 2006 |
Citation | Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006 | njamshidi | ISS | 16356931 | PMID: 16356931 |
Term | TBRXN:MYC1M2 Mycolic Acid Methyl Hydroxyl Addition - ISS | njamshidi | ISS | 16356931 | PMID: 16356931 F. Boissier, F. Bardou et al. Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. J. Biol. Chem. 2006 |
Citation | Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006 | njamshidi | IDA | 16356931 | PMID: 16356931 |
Citation | Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006 | njamshidi | IDA | 16356931 | PMID: 16356931 |
Term | TBRXN:MYC1M1 Mycolic Acid Methyl Hydroxyl Addition - IDA | njamshidi | IDA | 16356931 | PMID: 16356931 F. Boissier, F. Bardou et al. Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. J. Biol. Chem. 2006 |
Citation | Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. F. Boissier, F. Bardou et al. J. Biol. Chem. 2006 | njamshidi | ISS | 16356931 | PMID: 16356931 |
Term | TBRXN:MYC1M1 Mycolic Acid Methyl Hydroxyl Addition - ISS | njamshidi | ISS | 16356931 | PMID: 16356931 F. Boissier, F. Bardou et al. Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. J. Biol. Chem. 2006 |
Name | MmaA1 METHOXY MYCOLIC ACID SYNTHASE; trans cyclopropanation of methoxy- and ketomycolates | mjackson | IMP | | S-adenosyl-methionine-dependent mycolic acid methyltransferases |
Citation | Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. K. Takayama, C. Wang et al. Clin. Microbiol. Rev. 2005 | jjmcfadden | | 15653820 | Inferred from direct assay |
Term | EC:2.1.1.- Transferases. Transferring one-carbon groups. Methyltransferases. - NR | jjmcfadden | NR | | Inferred from direct assay K. Takayama, C. Wang et al. Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. Clin. Microbiol. Rev. 2005 |
Citation | MMAS-1, the branch point between cis- and trans-cyclopropane-containing oxygenated mycolates in Mycobacterium tuberculosis. authors,Y. Yuan,DC. Crane,JM. Musser,S. Sreevatsan,CE. Barry J. Biol. Chem. 1997 | extern:JZUCKER | | 9092547 | Inferred from experiment |
Term | EC:2.1.1.- Transferases. Transferring one-carbon groups. Methyltransferases. - NR | extern:JZUCKER | NR | | Inferred from experiment authors,Y. Yuan,DC. Crane,JM. Musser,S. Sreevatsan,CE. Barry MMAS-1, the branch point between cis- and trans-cyclopropane-containing oxygenated mycolates in Mycobacterium tuberculosis. J. Biol. Chem. 1997 |
Term | EC:2.1.1.79 Cyclopropane-fatty-acyl-phospholipid synthase. - NR | extern:JZUCKER | NR | | Inferred from experiment authors,Y. Yuan,DC. Crane,JM. Musser,S. Sreevatsan,CE. Barry MMAS-1, the branch point between cis- and trans-cyclopropane-containing oxygenated mycolates in Mycobacterium tuberculosis. J. Biol. Chem. 1997 |