Information on EC 2.3.1.128 - ribosomal-protein-alanine N-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.128
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RECOMMENDED NAME
GeneOntology No.
ribosomal-protein-alanine N-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein N-acetyl-L-alanine
show the reaction diagram
A group of enzymes in Escherichia coli that acetylate the N-terminal alanine residues of specific ribosomal proteins. cf. EC 2.3.1.88, peptide alpha-N-acetyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:ribosomal-protein-L-alanine N-acetyltransferase
A group of enzymes in Escherichia coli that acetylate the N-terminal alanine residues of specific ribosomal proteins. cf. EC 2.3.1.88, peptide alpha-N-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
113383-52-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K12
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Manually annotated by BRENDA team
strain K12
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + Ala-Arg-Tyr-Phe-Arg-Arg
CoA + ?
show the reaction diagram
a peptide substrate (S181-6) representing the first six N-terminal residues of S18 (minus the initiator methionine) is used as a substrate
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?
acetyl-CoA + ribosomal-protein L-alanine
CoA + ribosomal-protein N-acetyl-L-alanine
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + ribosomal-protein L-alanine
CoA + ribosomal-protein N-acetyl-L-alanine
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio fischeri (strain ATCC 700601 / ES114)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18230
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calculated from amino acid sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of RimI is determined in complex with CoA, AcCoA, and a CoA-S-acetyl-ARYFRR bisubstrate inhibitor. The structures are consistent with a direct nucleophilic addition-elimination mechanism with Glu103 and Tyr115 acting as the catalytic base and acid, respectively. The RimI-bisubstrate complex suggests that several residues change conformation upon interacting with the N terminus of S18, including Glu103, the proposed active site base, facilitating proton exchange and catalysis
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography and gel filtration using a HiPrep 26/60 Sephacryl S-200 high-resolution gel filtration column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a C-terminal decahistidine tagged fusion protein in Escherichia coli
gene rimI encoding enzyme acetylating ribosomal protein S18 cloned into a mini-F plasmid pRE432 and sequenced
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Show AA Sequence (8202 entries)
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