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Ligand pre-tRNAAsp

Basic Ligand Information

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Substrate (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.26.11

pre-tRNAAsp + H2O = ?

730939

-

3.1.26.5

pre-tRNAAsp + H2O = ?

710549, 715914

-

3.1.26.5

pre-tRNAAsp + H2O = mature tRNAAsp + 5'-oligonucleotide

134456, 134459

-

3.1.26.5

pre-tRNAAsp + H2O = tRNAAsp + 5'-oligoribonucleotide

134413, 134430, 709529, 664080, 709538

-

3.1.26.5

3 entries

4.6.1.22

pre-tRNAAsp + H2O = ?

682841

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (31 results)

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Show Turnover Number (31 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.26.5

0.02

-

catalyzed by RNase P RNA

134447

3.1.26.5

0.09

-

catalyzed by circular RNnase P RNA

134447

4.6.1.22

0.024

-

R60C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.1

-

R65C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.11

-

R7C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.15

-

D15C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.2

-

N61C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.22

-

R68C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.23

-

K64C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.23

-

wild-type, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.24

-

H3C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.26

-

D42C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.26

-

R62C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.27

-

E40C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.27

-

R45C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.27

-

R45C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.27

-

R60C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.27

-

R7C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.28

-

D15C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.28

-

R65C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.28

-

V46C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.29

-

K64C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.3

-

E40C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.3

-

H3C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.3

-

N61C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.31

-

Q38C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.32

-

V46C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.33

-

Q38C mutant, single turnover cleavage rate constant kobs

682841

4.6.1.22

0.34

-

R62C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.37

-

D42C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

682841

4.6.1.22

0.37

-

R68C mutant, single turnover cleavage rate constant kobs

682841

3.1.26.5

2 entries

4.6.1.22

29 entries

K_M Value (4 results)

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Show KM Value (4 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.26.5

0.00004

-

-

134456

3.1.26.5

0.00011

-

catalyzed by RNase P RNA

134447

3.1.26.5

0.00022

-

catalyzed by circular RNase P RNA

134447

3.1.26.5

32

-

-

134459

3.1.26.5

4 entries

References & Links

Literature References (12)

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Show Reference (12 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

134413

2471397

Ribonuclease P: an enzyme with a catalytic RNA subunit

1989

Altman, S.

Adv. Enzymol. Relat. Areas Mol. Biol.

62

1-36

134430

358197

Ribonuclease P: an enzyme with an essential RNA component

1978

Stark, B.C.; Kole, R.; Bowman, E.J.; Altman, S.

Proc. Natl. Acad. Sci. USA

75

3717-3721

134447

8643411

Generation and characterization of circular Bacillus subtilis RNase P RNA; activation by RNase P protein

1995

Puttaraju, M.; Beebe, J.A.; Niranjanakumari, S.; Been, M.D.; Fierke, C.A.

Nucleic Acids Symp. Ser.

33

92-94

134456

8631344

Purification and characterization of mitochondrial ribonuclease P from Aspergillus nidulans

1996

Lee, Y.C.; Lee, B.J.; Hwang, D.S.; Kang, H.S.

Eur. J. Biochem.

235

289-296

134459

-

The partial purification of Methanococcus jannaschii RNase P holoenzyme

1999

Andrews, A.J.; Brown, J.W.

Nucleic Acids Symp. Ser.

41

60-62

664080

16331973

The 5' leader of precursor tRNAAsp bound to the Bacillus subtilis RNase P holoenzyme has an extended conformation

2005

Rueda, D.; Hsieh, J.; Day-Storms, J.J.; Fierke, C.A.; Walter, N.G.

Biochemistry

44

16130-16139

682841

17299131

Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage

2007

Niranjanakumari, S.; Day-Storms, J.J.; Ahmed, M.; Hsieh, J.; Zahler, N.H.; Venters, R.A.; Fierke, C.A.

RNA

13

521-535

709529

19733182

Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA in

2009

Xu, Y.; Amero, C.D.; Pulukkunat, D.K.; Gopalan, V.; Foster, M.P.

J. Mol. Biol.

393

1043-1055

709538

19932118

Protein-precursor tRNA contact leads to sequence-specific recognition of 5 leaders by bacterial ribonuclease P

2010

Koutmou, K.S.; Zahler, N.H.; Kurz, J.C.; Campbell, F.E.; Harris, M.E.; Fierke, C.A.

J. Mol. Biol.

396

195-208

710549

19549719

Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate

2009

Hsieh, J.; Fierke, C.A.

RNA

15

1565-1577

715914

20434461

A divalent cation stabilizes the active conformation of the B. subtilis RNase P x pre-tRNA complex: a role for an inner-sphere metal ion in RNase P

2010

Hsieh, J.; Koutmou, K.S.; Rueda, D.; Koutmos, M.; Walter, N.G.; Fierke, C.A.

J. Mol. Biol.

400

38-51

730939

24249226

tRNA 3' processing in yeast involves tRNase Z, Rex1, and Rrp6

2014

Skowronek, E.; Grzechnik, P.; Spaeth, B.; Marchfelder, A.; Kufel, J.

RNA

20

115-130

Links to other databases for pre-tRNAAsp

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Show Links (1 entry)