Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Neurospora crassa and UniProt Accession P12063

for references in articles please use BRENDA:EC6.1.1.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Neurospora crassa
UNIPROT: P12063 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Neurospora crassa
The enzyme appears in selected viruses and cellular organisms
Synonyms
tyrosyl-trna synthetase, tyrrs, cyt-18, mitochondrial tyrosyl-trna synthetase, mini-tyrrs, tyrrss, tyrosyl trna synthetase, cyt-18 protein, mttyrrs, ldtyrrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYT-18
Tyrosyl-tRNA synthetase
-
CYT-18 protein
-
-
Tyrosine translase
-
-
-
-
Tyrosine tRNA synthetase
-
-
-
-
Tyrosine--tRNA ligase
-
-
-
-
Tyrosine-transfer ribonucleate synthetase
-
-
-
-
Tyrosine-transfer RNA ligase
-
-
-
-
Tyrosyl--tRNA ligase
-
-
-
-
Tyrosyl-transfer ribonucleate synthetase
-
-
-
-
Tyrosyl-transfer ribonucleic acid synthetase
-
-
-
-
Tyrosyl-transfer RNA synthetase
-
-
-
-
Tyrosyl-tRNA ligase
-
-
-
-
Tyrosyl-tRNA synthetase
-
-
-
-
TyrRS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Acylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-45-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
?
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
?
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CYT-18 also promotes self-splicing of group I intron RNAs by stabilizing the functional structure in the conserved core
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 4.5 A co-crystal structure of the Twort orf 142-I2 group I intron ribozyme bound to splicing-active, carboxy-terminally truncated CYT-18. Structure shows that the group I intron binds across the two subunits of the homodimeric protein with a newly evolved RNA-binding surface distinct from that which binds tRNATyr. This RNA binding surface provides an extended scaffold for the phosphodiester backbone of the conserved catalytic core of the intron RNA, allowing the protein to promote the splicing of a wide variety of group I introns. The group I intron-binding surface includes three small insertions and additional structural adaptations relative to non-splicing bacterial TyrRSs, indicating a multistep adaptation for splicing function
1.95 A crystal structure of mutant DELTA424-669 of CYT-18 protein. DELTA424-669 crystals are grown by sitting-drop vapor diffusion. The crystals are in space group C2 with unit cell dimensions: a = 104.88 A, b = 73.21 A, c = 56.79 A, beta = 111.35°
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate precipitation and on a heparin-Sepharose column
mutant DELTA424-669
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CYT-18 is expressed from the plasmid pEX560 in the Escherichia coli strain HMS174DE3
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paukstelis, P.J.; Coon, R.; Madabusi, L.; Nowakowski, J.; Monzingo, A.; Robertus, J.; Lambowitz, A.M.
A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
Mol. Cell
17
417-428
2005
Neurospora crassa
Manually annotated by BRENDA team
Paukstelis, P.J.; Chen, J.; Chase, E.; Lambowitz, A.M.; Golden, B.L.
Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA
Nature
451
94-97
2008
Neurospora crassa (P12063), Neurospora crassa
Manually annotated by BRENDA team
Chadee, A.B.; Bhaskaran, H.; Russell, R.
Protein roles in group I intron RNA folding: the tyrosyl-tRNA synthetase CYT-18 stabilizes the native state relative to a long-lived misfolded structure without compromising folding kinetics
J. Mol. Biol.
395
656-670
2010
Neurospora crassa (P12063), Neurospora crassa
Manually annotated by BRENDA team