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Information on EC 3.5.4.28 - S-adenosylhomocysteine deaminase
for references in articles please use BRENDA:EC3.5.4.28
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.4 In cyclic amidines
3.5.4.28 S-adenosylhomocysteine deaminase
The expected taxonomic range for this enzyme is: Bacteria, Archaea
showSynonyms
s-adenosylhomocysteine deaminase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deaminase, adenosylhomocysteine
-
-
-
-
MJ1541
TtzA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-homocysteine + H2O = S-inosyl-L-homocysteine + NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of amidines
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-homocysteine aminohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
125149-24-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
Substrates: catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold higher than with S-adenosyl-L-homocysteine or adenosine
Products: -
Products: -
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
Substrates: catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold higher than with S-adenosyl-L-homocysteine or adenosine
Products: -
Products: -
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
Substrates: major route of S-adenosylhomocysteine metabolism
Products: -
Products: -
?
terbuthylazine + H2O
terbuthylazine-2-hydroxy + HCl
-
Substrates: -
Products: -
Products: -
?
terbuthylazine + H2O
terbuthylazine-2-hydroxy + HCl
Rhizobium rhizogenes AT13
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
Substrates: major route of S-adenosylhomocysteine metabolism
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
Ni2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
Zn2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
additional information
metal-dependent enzyme. The metal can not be removed from the enzyme nor can the nature of the catalytic metal be established. Dialysis of the wild-type enzyme for 3 days against a dipicolinic acid containing buffer fails to show any lowering enzyme activity, again indicating that chelation is not able to remove the bound metal in the active site. The catalytic metal is not removed by EDTA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM, 45% loss of activity. 1 mM, 91% loss of activity
additional information
-
not inhibited by metal chelators, iodoacetamide and NEM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.299
terbuthylazine
-
pH and temperature not specified in the publication
0.16
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme Y136R
0.4
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme Y136R/E150R
1.1
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, wild-type enzyme
3.9
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme E150R
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme Y136R/E150R
2.7
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme Y136R
58.2
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme E150R
1300
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.3
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme Y136R/E150R
21
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme E150R
230
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, mutant enzyme Y136R
4400
S-adenosyl-L-homocysteine
pH and temperature not specified in the publication, wild-type enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
-
pH 4.0: about 50% of maximal activity, pH 10.0: about 80% of maximal activity
6.5 - 7.5
-
more than 90% of activity maximum at pH 6.5 and 7.5, rapid drop of activity below pH 6.0 and above 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
the enzyme is involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens
metabolism
-
the enzyme is closely related to terbuthylazine degradation in Agrobacterium rhizogenes AT13
metabolism
-
the enzyme is involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens
-
metabolism
Rhizobium rhizogenes AT13
-
the enzyme is closely related to terbuthylazine degradation in Agrobacterium rhizogenes AT13
-
Show AA Sequence and Transmembrane Helices (2882 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C294S
the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C
E150R
less thermostable than wild-type enzyme, stable for 10 min at 50°C
Y136R
less thermostable than wild-type enzyme, stable for 10 min at 50°C
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
10 min, mutant enzyme Y136R/E150R loses 65% of its activity, mutant enzyme Y136R loses 20% of its activity, mutant enzyme E150R loses% of its activity
60
10 min, wild-type enzyme loses 10% of its activity, mutant enzyme Y136R loses 60% of its activity, mutant enzyme E150R loses 75% of its activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zulty, J.J.; Speedie, M.K.
Purification and characterization of S-adenosylhomocysteine deaminase from streptonigrin-producing Streptomyces flocculus
J. Bacteriol.
171
6840-6844
1989
Streptomyces albus
brenda
Miller, D.; O'Brien, K.; Xu, H.; White, R.H.
Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-deoxyadenosine
J. Bacteriol.
196
1064-1072
2013
Methanocaldococcus jannaschii (Q58936), Methanocaldococcus jannaschii DSM 2661 (Q58936)
brenda
Liu, Y.; Liu, W.; Li, M.; Liu, S.; Peng, D.; Zhao, F.; Wu, X.; Tan, H.
Biodegradation characteristics and mechanism of terbuthylazine by the newly isolated Agrobacterium rhizogenes strain AT13
J. Hazard. Mater.
456
131664
2023
Rhizobium rhizogenes, Rhizobium rhizogenes AT13
brenda
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