Literature summary for 4.2.1.22 extracted from

Pazicni, S.; Lukat-Rodgers, G.S.; Oliveriusova, J.; Rees, K.A.; Parks, R.B.; Clark, R.W.; Rodgers, K.R.; Kraus, J.P.; Burstyn, J.N.
The redox behavior of the heme in cystathionine beta-synthase is sensitive to pH (2004), Biochemistry, 43, 14684-14695.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	recombinant	-

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	full-length Fe(III)-enzyme and truncated Fe(III) CBS-45	Homo sapiens

pH Range

pH Minimum	pH Maximum	Comment	Organism
7.2	9.3	pH 7.2: about 45% of maximal activity, pH 9.3: about 75% of maximal activity, full-length Fe(III)-enzyme and truncated Fe(III) CBS-45	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
heme	the heme favors the ferric state at lower pH and, in the presence of reductants, attains the ferric state via transient formation of the ferrous state. Fe(II)-enzyme and Fe(III)-enzyme are apparently interconverted by a proton-controlled internal electron transfer process	Homo sapiens
pyridoxal 5'-phosphate	-	Homo sapiens

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Release 2023.1 (January 2023)