EC Number | Application | Comment | Organism |
---|---|---|---|
6.1.1.1 | drug development | the enzyme is a promising target for development of novel selective inhibitors as putative antituberculosis drugs | Mycobacterium tuberculosis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.1.1.1 | additional information | prevention of beta-sheet formation by introducing point mutations in the loop sequence results in a rapid transition (below 20 ns) of the loop from its functional closed M-like structure to an inactive open O-like structure, i.e. rapid diffusion of the catalytic loop outside the active site | Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.1 | Mg2+ | required | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.1 | ATP + L-tyrosine + tRNATyr | Mycobacterium tuberculosis | - |
AMP + diphosphate + L-tyrosyl-tRNATyr | - |
? | |
6.1.1.1 | ATP + L-tyrosine + tRNATyr | Mycobacterium tuberculosis ATCC 25618 | - |
AMP + diphosphate + L-tyrosyl-tRNATyr | - |
? | |
6.1.1.1 | additional information | Mycobacterium tuberculosis | enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr | ? | - |
? | |
6.1.1.1 | additional information | Mycobacterium tuberculosis ATCC 25618 | enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.1 | Mycobacterium tuberculosis | P9WFT1 | - |
- |
6.1.1.1 | Mycobacterium tuberculosis ATCC 25618 | P9WFT1 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.1 | ATP + L-tyrosine + tRNATyr | - |
Mycobacterium tuberculosis | AMP + diphosphate + L-tyrosyl-tRNATyr | - |
? | |
6.1.1.1 | ATP + L-tyrosine + tRNATyr | - |
Mycobacterium tuberculosis ATCC 25618 | AMP + diphosphate + L-tyrosyl-tRNATyr | - |
? | |
6.1.1.1 | additional information | enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr | Mycobacterium tuberculosis | ? | - |
? | |
6.1.1.1 | additional information | enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr | Mycobacterium tuberculosis ATCC 25618 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.1.1.1 | homodimer | the MtTyrRS monomer contains three domains: the catalytic domain (1-248), the anticodon-binding domain (249-341), and the C-terminal domain (342-424), three-dimensional structure of the MtTyrRS dimer, overview | Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.1 | mtTyrRS | - |
Mycobacterium tuberculosis |
6.1.1.1 | Tyrosyl-tRNA synthetase | - |
Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.1 | ATP | - |
Mycobacterium tuberculosis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.1.1.1 | evolution | the enzyme belongs to class I of aminoacyl-tRNA synthetases | Mycobacterium tuberculosis |
6.1.1.1 | additional information | enzyme MtTyrRS contains the HIGH-like and KFGKS catalytic motifs that catalyze amino acid activation with ATP.The conformational mobility of MtTyrRS catalytic KFGKS loop is analyzed by 100-ns all-atoms molecular dynamics simulations of the free enzyme and its complexes with different substrates: tyrosine, ATP, and the tyrosyl-adenylate intermediate. In the closed state of the active site, the KFGKS loop, readily adopts different stable conformations depending on the type of bound substrate. The closed state of the loop is stabilized by dynamic formation of two antiparallel beta-sheets at flanking ends which hold the KFGKS fragment inside the active center. Molecular dynamics simulations, conformation of the MtTyrRS catalytic loop in substrate?bound states, detailed overview | Mycobacterium tuberculosis |
6.1.1.1 | physiological function | the flexibility and rapid dynamics of the wild-type aminoacyl-tRNA synthetase catalytic loop structure are crucial for formation of protein-substrate interactions and subsequently for overall enzyme functional activity, dynamic properties of the enzyme, overview | Mycobacterium tuberculosis |