Literature summary for 3.13.2.1 extracted from

Brzezinski, K.
S-Adenosyl-L-homocysteine hydrolase a structural perspective on the enzyme with two Rossmann-fold domains (2020), Biomolecules, 10, 1682 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Cytophaga hutchinsonii
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Rattus norvegicus
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Mycobacterium tuberculosis
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Plasmodium falciparum
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Lupinus luteus
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Homo sapiens
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Thermotoga maritima
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Bradyrhizobium elkanii
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Pseudomonas aeruginosa
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Mus musculus
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Trypanosoma brucei brucei
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Leishmania major
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Cryptosporidium parvum
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Acanthamoeba castellanii
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Naegleria fowleri
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Burkholderia pseudomallei
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Brucella abortus
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Elizabethkingia anophelis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
S-adenosyl-L-homocysteine + H2O	Cytophaga hutchinsonii	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Rattus norvegicus	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Mycobacterium tuberculosis	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Plasmodium falciparum	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Lupinus luteus	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Homo sapiens	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Thermotoga maritima	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Bradyrhizobium elkanii	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Pseudomonas aeruginosa	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Mus musculus	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Trypanosoma brucei brucei	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Leishmania major	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Cryptosporidium parvum	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Acanthamoeba castellanii	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Naegleria fowleri	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Burkholderia pseudomallei	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Brucella abortus	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Elizabethkingia anophelis	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Pseudomonas aeruginosa ATCC 15692	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Brucella abortus 2308	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Burkholderia pseudomallei 1710b	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Mycobacterium tuberculosis ATCC 25618	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Thermotoga maritima ATCC 43589	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Cryptosporidium parvum Iowa II	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Trypanosoma brucei brucei 927/4 GUTat10.1	-	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	Acanthamoeba castellanii NEFF	-	L-homocysteine + adenosine	-	?

Organism

Organism	UniProt	Comment	Textmining
Acanthamoeba castellanii	L8H6B5	-	-
Acanthamoeba castellanii NEFF	L8H6B5	-	-
Bradyrhizobium elkanii	A0A087WNH6	-	-
Brucella abortus	Q2YQX8	-	-
Brucella abortus 2308	Q2YQX8	-	-
Burkholderia pseudomallei	Q3JY79	-	-
Burkholderia pseudomallei 1710b	Q3JY79	-	-
Cryptosporidium parvum	Q5CPH1	-	-
Cryptosporidium parvum Iowa II	Q5CPH1	-	-
Cytophaga hutchinsonii	-	-	-
Elizabethkingia anophelis	A0A077EDS4	-	-
Homo sapiens	P23526	-	-
Leishmania major	Q4Q124	-	-
Lupinus luteus	Q9SP37	-	-
Mus musculus	P50247	-	-
Mycobacterium tuberculosis	P9WGV3	-	-
Mycobacterium tuberculosis ATCC 25618	P9WGV3	-	-
Naegleria fowleri	A0A1Z0YU84	-	-
Plasmodium falciparum	P50250	-	-
Pseudomonas aeruginosa	Q9I685	-	-
Pseudomonas aeruginosa ATCC 15692	Q9I685	-	-
Rattus norvegicus	P10760	-	-
Thermotoga maritima	O51933	-	-
Thermotoga maritima ATCC 43589	O51933	-	-
Trypanosoma brucei brucei	Q383X0	-	-
Trypanosoma brucei brucei 927/4 GUTat10.1	Q383X0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
S-adenosyl-L-homocysteine + H2O	-	Cytophaga hutchinsonii	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Rattus norvegicus	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Mycobacterium tuberculosis	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Plasmodium falciparum	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Lupinus luteus	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Homo sapiens	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Thermotoga maritima	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Bradyrhizobium elkanii	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Pseudomonas aeruginosa	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Mus musculus	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Trypanosoma brucei brucei	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Leishmania major	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Cryptosporidium parvum	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Acanthamoeba castellanii	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Naegleria fowleri	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Burkholderia pseudomallei	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Brucella abortus	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Elizabethkingia anophelis	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Pseudomonas aeruginosa ATCC 15692	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Brucella abortus 2308	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Burkholderia pseudomallei 1710b	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Mycobacterium tuberculosis ATCC 25618	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Thermotoga maritima ATCC 43589	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Cryptosporidium parvum Iowa II	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Trypanosoma brucei brucei 927/4 GUTat10.1	L-homocysteine + adenosine	-	?
S-adenosyl-L-homocysteine + H2O	-	Acanthamoeba castellanii NEFF	L-homocysteine + adenosine	-	?

Synonyms

Synonyms	Comment	Organism
S-adenosyl-L-homocysteine hydrolase	-	Cytophaga hutchinsonii
S-adenosyl-L-homocysteine hydrolase	-	Rattus norvegicus
S-adenosyl-L-homocysteine hydrolase	-	Mycobacterium tuberculosis
S-adenosyl-L-homocysteine hydrolase	-	Plasmodium falciparum
S-adenosyl-L-homocysteine hydrolase	-	Lupinus luteus
S-adenosyl-L-homocysteine hydrolase	-	Homo sapiens
S-adenosyl-L-homocysteine hydrolase	-	Thermotoga maritima
S-adenosyl-L-homocysteine hydrolase	-	Bradyrhizobium elkanii
S-adenosyl-L-homocysteine hydrolase	-	Pseudomonas aeruginosa
S-adenosyl-L-homocysteine hydrolase	-	Mus musculus
S-adenosyl-L-homocysteine hydrolase	-	Trypanosoma brucei brucei
S-adenosyl-L-homocysteine hydrolase	-	Leishmania major
S-adenosyl-L-homocysteine hydrolase	-	Cryptosporidium parvum
S-adenosyl-L-homocysteine hydrolase	-	Acanthamoeba castellanii
S-adenosyl-L-homocysteine hydrolase	-	Naegleria fowleri
S-adenosyl-L-homocysteine hydrolase	-	Burkholderia pseudomallei
S-adenosyl-L-homocysteine hydrolase	-	Brucella abortus
S-adenosyl-L-homocysteine hydrolase	-	Elizabethkingia anophelis
SAHase	-	Cytophaga hutchinsonii
SAHase	-	Rattus norvegicus
SAHase	-	Mycobacterium tuberculosis
SAHase	-	Plasmodium falciparum
SAHase	-	Lupinus luteus
SAHase	-	Homo sapiens
SAHase	-	Thermotoga maritima
SAHase	-	Bradyrhizobium elkanii
SAHase	-	Pseudomonas aeruginosa
SAHase	-	Mus musculus
SAHase	-	Trypanosoma brucei brucei
SAHase	-	Leishmania major
SAHase	-	Cryptosporidium parvum
SAHase	-	Acanthamoeba castellanii
SAHase	-	Naegleria fowleri
SAHase	-	Burkholderia pseudomallei
SAHase	-	Brucella abortus
SAHase	-	Elizabethkingia anophelis

Cofactor

Cofactor	Comment	Organism
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Cytophaga hutchinsonii
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Rattus norvegicus
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Mycobacterium tuberculosis
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Plasmodium falciparum
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Lupinus luteus
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Homo sapiens
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Thermotoga maritima
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Bradyrhizobium elkanii
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Pseudomonas aeruginosa
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Mus musculus
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Trypanosoma brucei brucei
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Leishmania major
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Cryptosporidium parvum
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Acanthamoeba castellanii
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Naegleria fowleri
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Burkholderia pseudomallei
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Brucella abortus
NAD+	the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank	Elizabethkingia anophelis

General Information

General Information	Comment	Organism
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Cytophaga hutchinsonii
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Rattus norvegicus
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Mycobacterium tuberculosis
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Plasmodium falciparum
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Lupinus luteus
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Homo sapiens
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Thermotoga maritima
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Bradyrhizobium elkanii
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Pseudomonas aeruginosa
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Mus musculus
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Trypanosoma brucei brucei
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Leishmania major
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Cryptosporidium parvum
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Acanthamoeba castellanii
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Naegleria fowleri
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Burkholderia pseudomallei
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Brucella abortus
physiological function	S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes	Elizabethkingia anophelis