Literature summary for 3.13.2.1 extracted from

Kusakabe, Y.; Ishihara, M.; Umeda, T.; Kuroda, D.; Nakanishi, M.; Kitade, Y.; Gouda, H.; Nakamura, K.T.; Tanaka, N.
Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase (2015), Sci. Rep., 5, 16641 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme SAHH in complex with adenosine and with two reaction intermediate analogues, 3'-keto-aristeromycin (3KA) and noraristeromycin (NRN), X-ray diffraction structure determination and analysis at resolutions of 1.55, 1.55, and 1.65 A, respectively	Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
RBV	an antiviral drug	Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Na+	activates, structure analysis of the cation-binding site in MmSAHH, overview	Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-homocysteine + H2O	Mus musculus	-	L-homocysteine + adenosine	-	r

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P50247	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme binds the reaction intermediate analogues 3'-oxo-aristeromycin (3KA) and noraristeromycin (NRN), and reacts with 3KA in a Michael addition	Mus musculus	?	-	?
S-adenosyl-L-homocysteine + H2O	-	Mus musculus	L-homocysteine + adenosine	-	r
S-adenosyl-L-homocysteine + H2O	reversible hydrolysis, five-step process of SAH hydrolysis by SAHH	Mus musculus	L-homocysteine + adenosine	-	r

Subunits

Subunits	Comment	Organism
homotetramer	4 * 48000, SDS-PAGE	Mus musculus
More	the subunit of MmSAHH consists of two large domains separated by a cleft containing a deep pocket, two hinge regions and a small C-terminal domain that is separate from the main body of the subunit and extends to the adjacent subunit. One of the large domains is responsible for cofactorbinding, and the other is necessary for substrate binding. The two large domains are unequal in size. The substrate-binding domain is larger and comprises 212 residues, whereas the cofactor-binding domain comprises 155 residues. Amino acid sequence comparisons	Mus musculus

Synonyms

Synonyms	Comment	Organism
S-adenosyl-L-homocysteine hydrolase	-	Mus musculus
SAH hydrolase	-	Mus musculus
SAHH	-	Mus musculus

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	the enzyme tetramer tightly but not covalently binds an NAD+ cofactor, binding structure, overview. The cofactor-binding domain comprises residues 197-351. The basic element of the secondary structure in this domain is a six-stranded parallel beta-sheet in the centre of the domain that is sandwiched by two arrays of three alpha-helices each. The six-stranded parallel beta-sheet is flanked by four alpha-helices and constitutes a characteristic dinucleotide-binding motif or Rossmann fold composed of two betaalphabetaalphabeta units	Mus musculus

General Information

General Information	Comment	Organism
evolution	S-adenosyl-L-homocysteine hydrolase (SAHH) is one of the most highly conserved enzymes across kingdoms	Mus musculus
additional information	the substrate-binding domain comprises residues 1-181 and 355-385. It is an alpha/beta-type structure consisting of eight alpha-helices and eight beta-strands. The structural core in the domain is an eight-stranded parallel beta-sheet in the centre of the domain that is sandwiched by two arrays of three alpha-helices each. Conformational changes upon substrate binding, overview	Mus musculus

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Release 2023.1 (January 2023)