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Literature summary extracted from

  • Joardar, A.; Jana, S.; Fitzek, E.; Gurha, P.; Majumder, M.; Chatterjee K, Geisler M, Gupta R.
    Role of forefinger and thumb loops in production of Psi54 and Psi55 in tRNAs by archaeal Pus10 (2013), RNA, 19, 1279-1294.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.25 wild-type and mutant enzymes, expression in Escherichia coli. Wild-type enzyme can produce both pseudouridine54 and pseudouridine55 in Escherichia coli tRNAs Methanocaldococcus jannaschii
5.4.99.B25 wild-type and mutant enzymes, expression in Escherichia coli. Wild-type enzyme can produce both pseudouridine54 and pseudouridine55 in Escherichia coli tRNAs Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
5.4.99.25 C106A/C109A decrease in tRNA pseudouridine54 synthase activity, no decrease in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 C106A/C109A decrease in tRNA pseudouridine54 synthase activity, no decrease in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 D275A the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 D275A the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 D277A decrease in tRNA pseudouridine54 synthase activity and low decrease in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 D277A decrease in tRNA pseudouridine54 synthase activity and low decrease in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 H376A/R377A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 H376A/R377A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 I412A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 I412A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 K413A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 K413A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 L440A the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 L440A the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 R273A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 R273A decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.25 Y339A the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii
5.4.99.B25 Y339A the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.25 Methanocaldococcus jannaschii Q60346
-
-
5.4.99.B25 Methanocaldococcus jannaschii Q60346
-
-
5.4.99.25 Methanocaldococcus jannaschii DSM 2661 Q60346
-
-
5.4.99.B25 Methanocaldococcus jannaschii DSM 2661 Q60346
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.B25 tRNA uridine54 the enzyme produces pseudouridine54 not only in tRNAPhe, but also in nearly all tRNAs. The enzyme also exhibts tRNA pseudouridine55 synthase activity. The forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its tRNA pseudouridine54 synthase, but not for its tRNA pseudouridine55 activity. A Leu residue, in addition to the catalytic Asp, is essential for both activities. Archaeal Pus10 proteins must use a different mechanism of recognition for tRNA pseudouridine55 than for the recognition of pseudouridine54. It is proposed that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. No mutation is detected that affects only tRNA pseudouridine54 synthase activity, both mechanisms for archaeal Pus10 activities must share some common features Methanocaldococcus jannaschii tRNA pseudouridine54
-
 ?
5.4.99.B25 tRNA uridine54 the enzyme produces pseudouridine54 not only in tRNAPhe, but also in nearly all tRNAs. The enzyme also exhibts tRNA pseudouridine55 synthase activity. The forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its tRNA pseudouridine54 synthase, but not for its tRNA pseudouridine55 activity. A Leu residue, in addition to the catalytic Asp, is essential for both activities. Archaeal Pus10 proteins must use a different mechanism of recognition for tRNA pseudouridine55 than for the recognition of pseudouridine54. It is proposed that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. No mutation is detected that affects only tRNA pseudouridine54 synthase activity, both mechanisms for archaeal Pus10 activities must share some common features Methanocaldococcus jannaschii DSM 2661 tRNA pseudouridine54
-
 ?
5.4.99.25 tRNA uridine55 the enzyme also exhibits tRNA pseudouridine54 synthase activity. The forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its tRNA pseudouridine54 synthase, but not for its tRNA pseudouridine55 activity. A Leu residue, in addition to the catalytic Asp, is essential for both activities. Archaeal Pus10 proteins must use a different mechanism of recognition for tRNA pseudouridine55 than for the recognition of pseudouridine54. It is proposed that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. No mutation mutation is detected that affects only tRNA pseudouridine54 synthase activity, both mechanisms for archaeal Pus10 activities must share some common features Methanocaldococcus jannaschii tRNA pseudouridine55
-
 ?
5.4.99.25 tRNA uridine55 the enzyme also exhibits tRNA pseudouridine54 synthase activity. The forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its tRNA pseudouridine54 synthase, but not for its tRNA pseudouridine55 activity. A Leu residue, in addition to the catalytic Asp, is essential for both activities. Archaeal Pus10 proteins must use a different mechanism of recognition for tRNA pseudouridine55 than for the recognition of pseudouridine54. It is proposed that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. No mutation mutation is detected that affects only tRNA pseudouridine54 synthase activity, both mechanisms for archaeal Pus10 activities must share some common features Methanocaldococcus jannaschii DSM 2661 tRNA pseudouridine55
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.4.99.25 MjPus10
-
 Methanocaldococcus jannaschii
5.4.99.B25 MjPus10
-
 Methanocaldococcus jannaschii