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show all sequences of 2.4.99.20

Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine nicotinic acid adenine dinucleotide phosphate (NAADP) synthesis and hydrolysis activities

Graeff, R.; Liu, Q.; Kriksunov, I.A.; Hao, Q.; Lee, H.C.; J. Biol. Chem. 281, 28951-28957 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Homo sapiens
Crystallization (Commentary)
Crystallization
Organism
complex of isoform CD38 with substrate NMN shows that the nicotinamide moiety is in close contact with Glu146 at 3.27 A and Asp155 at 2.52 A. Residue Asp147 is situated and directed away from the bound substrate
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
D147V
mutation has minimal effects on pH-dependence of the enzyme
Homo sapiens
D155N
mutation eliminates the strong pH dependence of the catalyzed reactions
Homo sapiens
D155Q
mutation eliminates the strong pH dependence of the catalyzed reactions; mutation preserves the strong pH dependence of the catalyzed reactions
Homo sapiens
E146A
mutation eliminates the strong pH dependence of the catalyzed reactions
Homo sapiens
E146G
mutation eliminates the strong pH dependence of the catalyzed reactions
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P28907
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
complex of isoform CD38 with substrate NMN shows that the nicotinamide moiety is in close contact with Glu146 at 3.27 A and Asp155 at 2.52 A. Residue Asp147 is situated and directed away from the bound substrate
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D147V
mutation has minimal effects on pH-dependence of the enzyme
Homo sapiens
D155N
mutation eliminates the strong pH dependence of the catalyzed reactions
Homo sapiens
D155Q
mutation eliminates the strong pH dependence of the catalyzed reactions; mutation preserves the strong pH dependence of the catalyzed reactions
Homo sapiens
E146A
mutation eliminates the strong pH dependence of the catalyzed reactions
Homo sapiens
E146G
mutation eliminates the strong pH dependence of the catalyzed reactions
Homo sapiens
Other publictions for EC 2.4.99.20
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
727515
Schmid
CD38: a NAADP degrading enzyme ...
Homo sapiens, Mus musculus
FEBS Lett.
585
3544-3548
2011
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2
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2
2
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727868
Rah
Generation of cyclic ADP-ribos ...
Mus musculus
J. Biol. Chem.
285
21877-21887
2010
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1
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1
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1
1
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726853
Moreschi
NAADP+ synthesis from cADPRP a ...
Aplysia californica, Axinella polypoides, Homo sapiens
Biochem. Biophys. Res. Commun.
345
573-580
2006
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3
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727857
Graeff
Acidic residues at the active ...
Homo sapiens
J. Biol. Chem.
281
28951-28957
2006
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1
1
5
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1
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5
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726898
Bacher
Channelling of substrate promi ...
Oryctolagus cuniculus
Biochem. J.
381
147-154
2004
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6
1
2
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1
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4
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6
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4
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724210
Chini
CD38 is the major enzyme respo ...
Mus musculus, Rattus norvegicus
Biochem. J.
362
125-130
2002
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4
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1
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3
3
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726647
Lee
ADP-ribosyl cyclase and CD38. ...
Aplysia californica, Homo sapiens
Adv. Exp. Med. Biol.
419
411-419
1997
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1
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8
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1
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727816
Aarhus
ADP-ribosyl cyclase and CD38 c ...
Aplysia californica, Homo sapiens
J. Biol. Chem.
270
30327-30333
1995
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2
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