The enzymes which catalyze the same reaction but have different amino acid compositions are commonly referred as :

Isoenzymes, also known as isozymes, are defined as different molecular forms of an enzyme that catalyze the same chemical reaction but differ in their primary structure, specifically their amino acid sequence [1]. These variations often arise from genetically determined differences, such as being encoded by different gene loci or resulting from alternative splicing [1]. Despite performing the same catalytic function, isoenzymes exhibit distinct physical and chemical properties, including different kinetic parameters (Km and Vmax), regulatory properties, and electrophoretic mobilities [2]. A classic example is Lactate Dehydrogenase (LDH), which exists in five isomeric forms with varying subunit compositions (H and M types) tailored for specific tissues like the heart or liver [2]. In contrast, isotopes refer to atomic variants, isomers to molecules with the same formula but different structures, and coenzymes to non-protein organic molecules that assist enzymes.

Sources

1. [1] https://iubmb.qmul.ac.uk/misc/isoen.html
2. [2] https://www.ncbi.nlm.nih.gov/books/NBK557536/